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Volumn 83, Issue , 2014, Pages 753-777

Small proteins can no longer be ignored

Author keywords

cell division; membrane; protein; signal transduction; sporulation; transport

Indexed keywords

CHAPERONE; MEMBRANE PROTEIN; PEPTIDOGLYCAN; PROTEIN; PROTEIN ACRZ; PROTEIN BLR; PROTEIN CMPA; PROTEIN CYDX; PROTEIN FBPB; PROTEIN FBPC; PROTEIN KDPF; PROTEIN MCIZ; PROTEIN MGTR; PROTEIN MNTS; PROTEIN PMRR; PROTEIN SDA; PROTEIN SGRT; PROTEIN SPOVM; REGULATOR PROTEIN; SMALL PROTEIN; SPACER DNA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; AMINO ACID; BACTERIAL PROTEIN; CODON; PROTEIN KINASE; RNA;

EID: 84902163304     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-070611-102400     Document Type: Review
Times cited : (263)

References (108)
  • 1
    • 0036493224 scopus 로고    scopus 로고
    • A question of size: The eukaryotic proteome and the problems in defining it
    • Harrison PM, Kumar A, Lang N, Snyder M, Gerstein M. 2002. A question of size: the eukaryotic proteome and the problems in defining it. Nucleic Acids Res. 30:1083-90
    • (2002) Nucleic Acids Res , vol.30 , pp. 1083-1090
    • Harrison, P.M.1    Kumar, A.2    Lang, N.3    Snyder, M.4    Gerstein, M.5
  • 2
    • 0030960992 scopus 로고    scopus 로고
    • Small open reading frames: Beautiful needles in the haystack
    • Basrai MA, Hieter P, Boeke JD. 1997. Small open reading frames: beautiful needles in the haystack. Genome Res. 7:768-71
    • (1997) Genome Res , vol.7 , pp. 768-771
    • Basrai, M.A.1    Hieter, P.2    Boeke, J.D.3
  • 3
    • 84902194588 scopus 로고    scopus 로고
    • What kind of data can be submitted to GenBank?
    • Natl. Cent. Biotechnol., Bethesda, Md
    • Natl. Cent. Biotechnol. 2011. What kind of data can be submitted to GenBank? In GenBank Submissions Handbook, Natl. Cent. Biotechnol., Bethesda, Md.
    • (2011) GenBank Submissions Handbook
  • 5
    • 57349189421 scopus 로고    scopus 로고
    • Small toxic proteins and the antisense RNAs that repress them
    • Fozo EM, Hemm MR, Storz G. 2008. Small toxic proteins and the antisense RNAs that repress them. Microbiol. Mol. Biol. Rev. 72:579-89
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 579-589
    • Fozo, E.M.1    Hemm, M.R.2    Storz, G.3
  • 6
    • 84880372200 scopus 로고    scopus 로고
    • High-resolution view of bacteriophage Gene expression by ribosome profiling
    • Liu X, Jiang H, Gu Z, Roberts JW. 2013. High-resolution view of bacteriophage ? gene expression by ribosome profiling. Proc. Natl. Acad. Sci. USA 110:11928-33
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11928-11933
    • Liu, X.1    Jiang, H.2    Gu, Z.3    Roberts, J.W.4
  • 8
    • 0030457111 scopus 로고    scopus 로고
    • Molecular genetics of sporulation in Bacillus subtilis
    • Stragier P, Losick R. 1996. Molecular genetics of sporulation in Bacillus subtilis. Annu. Rev. Genet. 30:297-341
    • (1996) Annu. Rev. Genet , vol.30 , pp. 297-341
    • Stragier, P.1    Losick, R.2
  • 9
    • 34047126471 scopus 로고    scopus 로고
    • I will survive: DNA protection in bacterial spores
    • Setlow P. 2007. I will survive: DNA protection in bacterial spores. Trends Microbiol. 15:172-80
    • (2007) Trends Microbiol , vol.15 , pp. 172-180
    • Setlow, P.1
  • 10
    • 0023464755 scopus 로고
    • Genetic analysis of Bacillus subtilis spo mutations generated by Tn917-mediated insertional mutagenesis
    • Sandman K, Losick R, Youngman P. 1987. Genetic analysis of Bacillus subtilis spo mutations generated by Tn917-mediated insertional mutagenesis. Genetics 117:603-17
    • (1987) Genetics , vol.117 , pp. 603-617
    • Sandman, K.1    Losick, R.2    Youngman, P.3
  • 12
    • 84867988931 scopus 로고    scopus 로고
    • Genomic determinants of sporulation in Bacilli and Clostridia: Towards the minimal set of sporulation-specific genes
    • Galperin MY, Mekhedov SL, Puigbo P, Smirnov S,Wolf YI, Rigden DJ. 2012. Genomic determinants of sporulation in Bacilli and Clostridia: towards the minimal set of sporulation-specific genes. Environ. Microbiol. 14:2870-90
    • (2012) Environ. Microbiol , vol.14 , pp. 2870-2890
    • Galperin, M.Y.1    Mekhedov, S.L.2    Puigbo, P.3    Smirnov, S.4    Wolf, Y.I.5    Rigden, D.J.6
  • 13
    • 56749151013 scopus 로고    scopus 로고
    • Small membrane proteins found by comparative genomics and ribosome binding site models
    • Hemm MR, Paul BJ, Schneider TD, Storz G, Rudd KE. 2008. Small membrane proteins found by comparative genomics and ribosome binding site models. Mol. Microbiol. 70:1487-501
    • (2008) Mol. Microbiol , vol.70 , pp. 1487-1501
    • Hemm, M.R.1    Paul, B.J.2    Schneider, T.D.3    Storz, G.4    Rudd, K.E.5
  • 14
    • 0037317673 scopus 로고    scopus 로고
    • Subcellular localization of a small sporulation protein in Bacillus subtilis
    • van Ooij C, Losick R. 2003. Subcellular localization of a small sporulation protein in Bacillus subtilis. J. Bacteriol. 185:1391-98
    • (2003) J. Bacteriol , vol.185 , pp. 1391-1398
    • Van Ooij, C.1    Losick, R.2
  • 15
    • 0034718116 scopus 로고    scopus 로고
    • Structural and functional studies on an FtsH inhibitor from Bacillus subtilis
    • Prajapati RS, Ogura T, Cutting SM. 2000. Structural and functional studies on an FtsH inhibitor from Bacillus subtilis. Biochim. Biophys. Acta 1475:353-59
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 353-359
    • Prajapati, R.S.1    Ogura, T.2    Cutting, S.M.3
  • 16
    • 33751355259 scopus 로고    scopus 로고
    • Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis
    • Ramamurthi KS, Clapham KR, Losick R. 2006. Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis. Mol. Microbiol. 62:1547-57
    • (2006) Mol. Microbiol , vol.62 , pp. 1547-1557
    • Ramamurthi, K.S.1    Clapham, K.R.2    Losick, R.3
  • 17
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi KS, Lecuyer S, Stone HA, Losick R. 2009. Geometric cue for protein localization in a bacterium. Science 323:1354-57
    • (2009) Science , vol.323 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 18
    • 0026567712 scopus 로고
    • Characterization of spoIVA, a sporulation gene involved in coat morphogenesis in Bacillus subtilis
    • Roels S, Driks A, Losick R. 1992. Characterization of spoIVA, a sporulation gene involved in coat morphogenesis in Bacillus subtilis. J. Bacteriol. 174:575-85
    • (1992) J. Bacteriol , vol.174 , pp. 575-585
    • Roels, S.1    Driks, A.2    Losick, R.3
  • 19
    • 48349096860 scopus 로고    scopus 로고
    • ATP-driven self-Assembly of amorphogenetic protein in Bacillus subtilis
    • Ramamurthi KS, Losick R. 2008. ATP-driven self-Assembly of amorphogenetic protein in Bacillus subtilis. Mol. Cell 31:406-14
    • (2008) Mol. Cell , vol.31 , pp. 406-414
    • Ramamurthi, K.S.1    Losick, R.2
  • 20
    • 84872202500 scopus 로고    scopus 로고
    • ATP hydrolysis by a domain related to translation factor GTPases drives polymerization of a static bacterial morphogenetic protein
    • Castaing JP, Nagy A, Anantharaman V, Aravind L, Ramamurthi KS. 2013. ATP hydrolysis by a domain related to translation factor GTPases drives polymerization of a static bacterial morphogenetic protein. Proc. Natl. Acad. Sci. USA 110:E151-60
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110
    • Castaing, J.P.1    Nagy, A.2    Anantharaman, V.3    Aravind, L.4    Ramamurthi, K.S.5
  • 21
    • 0030928663 scopus 로고    scopus 로고
    • SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH
    • Cutting S, Anderson M, LysenkoE, Page A,TomoyasuT, et al. 1997. SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH. J. Bacteriol. 179:5534-42
    • (1997) J. Bacteriol , vol.179 , pp. 5534-5542
    • Cutting, S.1    Anderson, M.2    Lysenko, E.3    Page, A.4    Tomoyasu, T.5
  • 22
    • 34547929879 scopus 로고    scopus 로고
    • Phage lambda CIII: A protease inhibitor regulating the lysis-lysogeny decision
    • Kobiler O, Rokney A, Oppenheim AB. 2007. Phage lambda CIII: a protease inhibitor regulating the lysis-lysogeny decision. PLoS ONE 2:e363
    • (2007) PLoS ONE , vol.2
    • Kobiler, O.1    Rokney, A.2    Oppenheim, A.B.3
  • 23
    • 51749104418 scopus 로고    scopus 로고
    • Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli ?32 by ?CIII
    • Halder S, Banerjee S, Parrack P. 2008. Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli ?32 by ?CIII. FEBS J. 275:4767-72
    • (2008) FEBS J , vol.275 , pp. 4767-4772
    • Halder, S.1    Banerjee, S.2    Parrack, P.3
  • 24
    • 65649111204 scopus 로고    scopus 로고
    • The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease
    • Le AT, SchumannW. 2009. The Spo0E phosphatase of Bacillus subtilis is a substrate of the FtsH metalloprotease. Microbiology 155:1122-32
    • (2009) Microbiology , vol.155 , pp. 1122-1132
    • Le, A.T.1    Schumann, W.2
  • 25
    • 84867466822 scopus 로고    scopus 로고
    • The biofilm formation defect of a Bacillus subtilis flotillin-defective mutant involves the protease FtsH
    • Yepes A, Schneider J, Mielich B, Koch G, Garc?́a-Betancur JC, et al. 2012. The biofilm formation defect of a Bacillus subtilis flotillin-defective mutant involves the protease FtsH. Mol. Microbiol. 86:457-71
    • (2012) Mol. Microbiol , vol.86 , pp. 457-471
    • Yepes, A.1    Schneider, J.2    Mielich, B.3    Koch, G.4    Garća-Betancur, J.C.5
  • 26
    • 0015358085 scopus 로고
    • Sporulation in Bacillus subtilis Characterization of oligosporogenous mutants and comparison of their phenotypes with those of asporogenous mutants
    • Coote JG. 1972. Sporulation in Bacillus subtilis. Characterization of oligosporogenous mutants and comparison of their phenotypes with those of asporogenous mutants. J. Gen. Microbiol. 71:1-15
    • (1972) J. Gen. Microbiol , vol.71 , pp. 1-15
    • Coote, J.G.1
  • 27
    • 84860593197 scopus 로고    scopus 로고
    • Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis
    • Ebmeier SE, Tan IS, Clapham KR, Ramamurthi KS. 2012. Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis. Mol. Microbiol. 84:682-96
    • (2012) Mol. Microbiol , vol.84 , pp. 682-696
    • Ebmeier, S.E.1    Tan, I.S.2    Clapham, K.R.3    Ramamurthi, K.S.4
  • 28
    • 77957832370 scopus 로고    scopus 로고
    • Small genes under sporulation control in the Bacillus subtilis genome
    • Schmalisch M, Maiques E,Nikolov L, Camp AH,Chevreux B, et al. 2010. Small genes under sporulation control in the Bacillus subtilis genome. J. Bacteriol. 192:5402-12
    • (2010) J. Bacteriol , vol.192 , pp. 5402-5412
    • Schmalisch, M.1    Maiques, E.2    Nikolov, L.3    Camp, A.H.4    Chevreux, B.5
  • 29
    • 84874693324 scopus 로고    scopus 로고
    • SpoIVA and SipL are Clostridium difficile spore morphogenetic proteins
    • Putnam EE, Nock AM, Lawley TD, Shen A. 2013. SpoIVA and SipL are Clostridium difficile spore morphogenetic proteins. J. Bacteriol. 195:1214-25
    • (2013) J. Bacteriol , vol.195 , pp. 1214-1225
    • Putnam, E.E.1    Nock, A.M.2    Lawley, T.D.3    Shen, A.4
  • 30
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: From Z ring to divisome
    • Lutkenhaus J, Pichoff S, Du S. 2012. Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton 69:778-90
    • (2012) Cytoskeleton , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 31
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M. 2010. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74:504-28
    • (2010) Microbiol. Mol. Biol. Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 33
    • 0037133943 scopus 로고    scopus 로고
    • Asymmetric cell division in B subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ
    • Ben-Yehuda S, Losick R. 2002. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ. Cell 109:257-66
    • (2002) Cell , vol.109 , pp. 257-266
    • Ben-Yehuda, S.1    Losick, R.2
  • 34
    • 0029918758 scopus 로고    scopus 로고
    • Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis
    • Levin PA, Losick R. 1996. Transcription factor Spo0A switches the localization of the cell division protein FtsZ from a medial to a bipolar pattern in Bacillus subtilis. Genes Dev. 10:478-88
    • (1996) Genes Dev , vol.10 , pp. 478-488
    • Levin, P.A.1    Losick, R.2
  • 35
    • 41749098049 scopus 로고    scopus 로고
    • Peptide inhibitor of cytokinesis during sporulation in Bacillus subtilis
    • Handler AA, Lim JE, Losick R. 2008. Peptide inhibitor of cytokinesis during sporulation in Bacillus subtilis. Mol. Microbiol. 68:588-99
    • (2008) Mol. Microbiol , vol.68 , pp. 588-599
    • Handler, A.A.1    Lim, J.E.2    Losick, R.3
  • 36
    • 0034283007 scopus 로고    scopus 로고
    • CtrA mediates a DNA replication checkpoint that prevents cell division in Caulobacter crescentus
    • Wortinger M, Sackett MJ, Brun YV. 2000. CtrA mediates a DNA replication checkpoint that prevents cell division in Caulobacter crescentus. EMBO J. 19:4503-12
    • (2000) EMBO J , vol.19 , pp. 4503-4512
    • Wortinger, M.1    Sackett, M.J.2    Brun, Y.V.3
  • 37
    • 79959677792 scopus 로고    scopus 로고
    • A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW
    • Modell JW, Hopkins AC, Laub MT. 2011. A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW. Genes Dev. 25:1328-43
    • (2011) Genes Dev , vol.25 , pp. 1328-1343
    • Modell, J.W.1    Hopkins, A.C.2    Laub, M.T.3
  • 38
    • 84859619053 scopus 로고    scopus 로고
    • SulA inhibits assembly of FtsZ by a simple sequestration mechanism
    • Chen Y, Milam SL, Erickson HP. 2012. SulA inhibits assembly of FtsZ by a simple sequestration mechanism. Biochemistry 51:3100-9
    • (2012) Biochemistry , vol.51 , pp. 3100-3109
    • Chen, Y.1    Milam, S.L.2    Erickson, H.P.3
  • 39
    • 79955007775 scopus 로고    scopus 로고
    • Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane
    • Mohammadi T, van Dam V, Sijbrandi R, Vernet T, Zapun A, et al. 2011. Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J. 30:1425-32
    • (2011) EMBO J , vol.30 , pp. 1425-1432
    • Mohammadi, T.1    Van Dam, V.2    Sijbrandi, R.3    Vernet, T.4    Zapun, A.5
  • 40
    • 70849086538 scopus 로고    scopus 로고
    • Why and how bacteria localize proteins
    • Shapiro L, McAdamsHH, Losick R. 2009. Why and how bacteria localize proteins. Science 326:1225-28
    • (2009) Science , vol.326 , pp. 1225-1228
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 41
    • 0033913572 scopus 로고    scopus 로고
    • Intergenic blr gene in Escherichia coli encodes a 41-residue membrane protein affecting intrinsic susceptibility to certain inhibitors of peptidoglycan synthesis
    • Wong RS, McMurry LM, Levy SB. 2000. "Intergenic" blr gene in Escherichia coli encodes a 41-residue membrane protein affecting intrinsic susceptibility to certain inhibitors of peptidoglycan synthesis. Mol. Microbiol. 37:364-70
    • (2000) Mol. Microbiol , vol.37 , pp. 364-370
    • Wong, R.S.1    McMurry, L.M.2    Levy, S.B.3
  • 42
    • 73849131808 scopus 로고    scopus 로고
    • Small RNAs and small proteins involved in resistance to cell envelope stress and acid shock in Escherichia coli: Analysis of a bar-coded mutant collection
    • Hobbs EC, Astarita JL, Storz G. 2010. Small RNAs and small proteins involved in resistance to cell envelope stress and acid shock in Escherichia coli: analysis of a bar-coded mutant collection. J. Bacteriol. 192:59-67
    • (2010) J. Bacteriol , vol.192 , pp. 59-67
    • Hobbs, E.C.1    Astarita, J.L.2    Storz, G.3
  • 43
    • 84868602418 scopus 로고    scopus 로고
    • The ?-lactam resistance protein Blr, a small membrane polypeptide, is a component of the Escherichia coli cell division machinery
    • Karimova G, Davi M, Ladant D. 2012. The ?-lactam resistance protein Blr, a small membrane polypeptide, is a component of the Escherichia coli cell division machinery. J. Bacteriol. 194:5576-88
    • (2012) J. Bacteriol , vol.194 , pp. 5576-5588
    • Karimova, G.1    Davi, M.2    Ladant, D.3
  • 44
    • 0342546514 scopus 로고    scopus 로고
    • - translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro
    • - translocating Kdp complex of Escherichia coli and is responsible for stabilization of the complex in vitro. J. Biol. Chem. 274:37901-7
    • (1999) J. Biol. Chem , vol.274 , pp. 37901-37907
    • Gabel, M.1    Möllenkamp, T.2    Puppe, W.3    Altendorf, K.4
  • 45
    • 41549157360 scopus 로고    scopus 로고
    • Reduction of turgor is not the stimulus for the sensor kinase KdpD of Escherichia coli
    • Hamann K, Zimmann P, Altendorf K. 2008. Reduction of turgor is not the stimulus for the sensor kinase KdpD of Escherichia coli. J. Bacteriol. 190:2360-67
    • (2008) J. Bacteriol , vol.190 , pp. 2360-2367
    • Hamann, K.1    Zimmann, P.2    Altendorf, K.3
  • 46
    • 84875929356 scopus 로고    scopus 로고
    • Overexpression of the KdpF membrane peptide in Mycobacterium bovis BCG results in reduced intramacrophage growth and altered coding morphology
    • Gannoun-Zaki L, Alibaud L, Carrére-Kremer S, Kremer L, Blanc-Potard AB. 2013. Overexpression of the KdpF membrane peptide in Mycobacterium bovis BCG results in reduced intramacrophage growth and altered coding morphology. PLoS ONE 8:e60379
    • (2013) PLoS ONE , vol.8
    • Gannoun-Zaki, L.1    Alibaud, L.2    Carrére-Kremer, S.3    Kremer, L.4    Blanc-Potard, A.B.5
  • 47
    • 84867374260 scopus 로고    scopus 로고
    • Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance
    • Hobbs EC, Yin X, Paul BJ, Astarita JL, Storz G. 2012. Conserved small protein associates with the multidrug efflux pump AcrB and differentially affects antibiotic resistance. Proc. Natl. Acad. Sci. USA 109:16696-701
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 16696-16701
    • Hobbs, E.C.1    Yin, X.2    Paul, B.J.3    Astarita, J.L.4    Storz, G.5
  • 49
    • 8544271637 scopus 로고    scopus 로고
    • Involvement of a novel transcriptional activator and small RNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phophotransferase system
    • Vanderpool CK, Gottesman S. 2004. Involvement of a novel transcriptional activator and small RNA in post-transcriptional regulation of the glucose phosphoenolpyruvate phophotransferase system. Mol. Microbiol. 54:1076-89
    • (2004) Mol. Microbiol , vol.54 , pp. 1076-1089
    • Vanderpool, C.K.1    Gottesman, S.2
  • 50
    • 38049115217 scopus 로고    scopus 로고
    • A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide
    • Wadler CS, Vanderpool CK. 2007. A dual function for a bacterial small RNA: SgrS performs base pairing-dependent regulation and encodes a functional polypeptide. Proc. Natl. Acad. Sci. USA 104:20454-59
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 20454-20459
    • Wadler, C.S.1    Vanderpool, C.K.2
  • 51
    • 33947139094 scopus 로고    scopus 로고
    • The novel transcription factor SgrR coordinates the response to glucose-phosphate stress
    • Vanderpool CK, Gottesman S. 2007. The novel transcription factor SgrR coordinates the response to glucose-phosphate stress. J. Bacteriol. 189:2238-48
    • (2007) J. Bacteriol , vol.189 , pp. 2238-2248
    • Vanderpool, C.K.1    Gottesman, S.2
  • 52
    • 84902199130 scopus 로고    scopus 로고
    • Characterization of the interaction between the small regulatory peptide SgrT and the EIICBGlu of the glucose-phosphotransferase system of E. Coli K-12
    • Kosfeld A, Jahreis K. 2012. Characterization of the interaction between the small regulatory peptide SgrT and the EIICBGlu of the glucose- phosphotransferase system of E. coli K-12. Metabolites 2:756-74
    • (2012) Metabolites , vol.2 , pp. 756-774
    • Kosfeld, A.1    Jahreis, K.2
  • 53
    • 1042290470 scopus 로고    scopus 로고
    • The low molecular mass subunits of the photosynthetic supracomplex, photosystem II
    • Shi LX, Schr öder WP. 2004. The low molecular mass subunits of the photosynthetic supracomplex, photosystem II. Biochim. Biophys. Acta 1608:75-96
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 75-96
    • Shi, L.X.1    Schr Öder, W.P.2
  • 54
    • 33846796241 scopus 로고    scopus 로고
    • PetG and PetN, but not PetL, are essential subunits of the cytochrome b6f complex from Synechocystis PCC 6803
    • Schneider D, Volkmer T, Rögner M. 2007. PetG and PetN, but not PetL, are essential subunits of the cytochrome b6f complex from Synechocystis PCC 6803. Res. Microbiol. 158:45-50
    • (2007) Res. Microbiol , vol.158 , pp. 45-50
    • Schneider, D.1    Volkmer, T.2    Rögner, M.3
  • 55
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of photosystems i and II
    • Nelson N, Yocum CF. 2006. Structure and function of photosystems I and II. Annu. Rev. Plant Biol. 57:521-65
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 56
    • 84880988082 scopus 로고    scopus 로고
    • The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity
    • Vanorsdel CE, Bhatt S, Allen RJ, Brenner EP, Hobson JJ, et al. 2013. The Escherichia coli CydX protein is a member of the CydAB cytochrome bd oxidase complex and is required for cytochrome bd oxidase activity. J. Bacteriol. 195:3640-50
    • (2013) J. Bacteriol , vol.195 , pp. 3640-3650
    • Vanorsdel, C.E.1    Bhatt, S.2    Allen, R.J.3    Brenner, E.P.4    Hobson, J.J.5
  • 58
    • 84866872924 scopus 로고    scopus 로고
    • Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide
    • Kato A, Chen HD, Latifi T, Groisman EA. 2012. Reciprocal control between a bacterium's regulatory system and the modification status of its lipopolysaccharide. Mol. Cell 47:897-908
    • (2012) Mol. Cell , vol.47 , pp. 897-908
    • Kato, A.1    Chen, H.D.2    Latifi, T.3    Groisman, E.A.4
  • 59
    • 62949231327 scopus 로고    scopus 로고
    • Hydrophobic peptides: Novel regulators within bacterial membrane
    • Alix E, Blanc-Potard AB. 2009. Hydrophobic peptides: novel regulators within bacterial membrane. Mol. Microbiol. 72:5-11
    • (2009) Mol. Microbiol , vol.72 , pp. 5-11
    • Alix, E.1    Blanc-Potard, A.B.2
  • 60
    • 77953523940 scopus 로고    scopus 로고
    • Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides
    • Herrera CM, Hankins JV, Trent MS. 2010. Activation of PmrA inhibits LpxT-dependent phosphorylation of lipid A promoting resistance to antimicrobial peptides. Mol. Microbiol. 76:1444-60
    • (2010) Mol. Microbiol , vol.76 , pp. 1444-1460
    • Herrera, C.M.1    Hankins, J.V.2    Trent, M.S.3
  • 61
    • 38949185102 scopus 로고    scopus 로고
    • Peptide-Assisted degradation of the Salmonella MgtC virulence factor
    • Alix E, Blanc-Potard AB. 2008. Peptide-Assisted degradation of the Salmonella MgtC virulence factor. EMBO J. 27:546-57
    • (2008) EMBO J , vol.27 , pp. 546-557
    • Alix, E.1    Blanc-Potard, A.B.2
  • 62
    • 36049046412 scopus 로고    scopus 로고
    • Stimulus-dependent differential regulation in the Escherichia coli PhoQPhoP system
    • Miyashiro T, Goulian M. 2007. Stimulus-dependent differential regulation in the Escherichia coli PhoQPhoP system. Proc. Natl. Acad. Sci. USA 104:16305-10
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16305-16310
    • Miyashiro, T.1    Goulian, M.2
  • 63
    • 72049119860 scopus 로고    scopus 로고
    • A PhoQ/P-regulated small RNA regulates sensitivity of Escherichia coli to antimicrobial peptides
    • Moon K, Gottesman S. 2009. A PhoQ/P-regulated small RNA regulates sensitivity of Escherichia coli to antimicrobial peptides. Mol. Microbiol. 74:1314-30
    • (2009) Mol. Microbiol , vol.74 , pp. 1314-1330
    • Moon, K.1    Gottesman, S.2
  • 64
    • 0031821817 scopus 로고    scopus 로고
    • Magnesium and the role of MgtC in growth of Salmonella typhimurium
    • Moncrief MB, Maguire ME. 1998. Magnesium and the role of MgtC in growth of Salmonella typhimurium. Infect. Immun. 66:3802-9
    • (1998) Infect. Immun , vol.66 , pp. 3802-3809
    • Moncrief, M.B.1    Maguire, M.E.2
  • 65
    • 84879919792 scopus 로고    scopus 로고
    • A bacterial virulence protein promotes pathogenicity by inhibiting the bacterium's own F1F0 ATP synthase
    • Lee EJ, Pontes MH, Groisman EA. 2013. A bacterial virulence protein promotes pathogenicity by inhibiting the bacterium's own F1F0 ATP synthase. Cell 154:146-56
    • (2013) Cell , vol.154 , pp. 146-156
    • Lee, E.J.1    Pontes, M.H.2    Groisman, E.A.3
  • 67
    • 74249107490 scopus 로고    scopus 로고
    • Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide
    • Lippa AM, Goulian M. 2009. Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide. PLoS Genet. 5:e1000788
    • (2009) PLoS Genet , vol.5
    • Lippa, A.M.1    Goulian, M.2
  • 68
    • 84857941860 scopus 로고    scopus 로고
    • Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli
    • Lippa AM, Goulian M. 2012. Perturbation of the oxidizing environment of the periplasm stimulates the PhoQ/PhoP system in Escherichia coli. J. Bacteriol. 194:1457-63
    • (2012) J. Bacteriol , vol.194 , pp. 1457-1463
    • Lippa, A.M.1    Goulian, M.2
  • 69
    • 84877976271 scopus 로고    scopus 로고
    • DsbA and MgrB regulate steA expression through the two-component system PhoQ/PhoP in Salmonella enterica
    • Cardenal-Mun∼oz E, Ramos-Morales F. 2013. DsbA and MgrB regulate steA expression through the two-component system PhoQ/PhoP in Salmonella enterica. J. Bacteriol. 195:2368-78
    • (2013) J. Bacteriol , vol.195 , pp. 2368-2378
    • Cardenal-Munoz, E.1    Ramos-Morales, F.2
  • 70
    • 0035951415 scopus 로고    scopus 로고
    • Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis
    • Burkholder WF,Kurtser I, Grossman AD. 2001. Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis. Cell 104:269-79
    • (2001) Cell , vol.104 , pp. 269-279
    • Burkholder, W.F.1    Kurtser, I.2    Grossman, A.D.3
  • 71
    • 1642271608 scopus 로고    scopus 로고
    • Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis
    • Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF. 2004. Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis. Mol. Cell 13:689-701
    • (2004) Mol. Cell , vol.13 , pp. 689-701
    • Rowland, S.L.1    Burkholder, W.F.2    Cunningham, K.A.3    Maciejewski, M.W.4    Grossman, A.D.5    King, G.F.6
  • 72
    • 33947638546 scopus 로고    scopus 로고
    • The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition
    • Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, et al. 2007. The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J. Mol. Biol. 368:407-20
    • (2007) J. Mol. Biol , vol.368 , pp. 407-420
    • Whitten, A.E.1    Jacques, D.A.2    Hammouda, B.3    Hanley, T.4    King, G.F.5
  • 73
    • 58449094352 scopus 로고    scopus 로고
    • The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F
    • Cunningham KA, Burkholder WF. 2009. The histidine kinase inhibitor Sda binds near the site of autophosphorylation and may sterically hinder autophosphorylation and phosphotransfer to Spo0F. Mol. Microbiol. 71:659-77
    • (2009) Mol. Microbiol , vol.71 , pp. 659-677
    • Cunningham, K.A.1    Burkholder, W.F.2
  • 74
    • 58849159963 scopus 로고    scopus 로고
    • How to switch off a histidine kinase: Crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda
    • Bick MJ, Lamour V, Rajashankar KR, Gordiyenko Y, Robinson CV, Darst SA. 2009. How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda. J. Mol. Biol. 386:163-77
    • (2009) J. Mol. Biol , vol.386 , pp. 163-177
    • Bick, M.J.1    Lamour, V.2    Rajashankar, K.R.3    Gordiyenko, Y.4    Robinson, C.V.5    Darst, S.A.6
  • 75
    • 66249132335 scopus 로고    scopus 로고
    • Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state
    • Jacques DA, Streamer M, Rowland SL, King GF, Guss JM, et al. 2009. Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallogr. D 65:574-81
    • (2009) Acta Crystallogr D , vol.65 , pp. 574-581
    • Jacques, D.A.1    Streamer, M.2    Rowland, S.L.3    King, G.F.4    Guss, J.M.5
  • 78
    • 80055048346 scopus 로고    scopus 로고
    • The Escherichia coli MntR miniregulon includes genes encoding a small protein and an efflux pump required for manganese homeostasis
    • Waters LS, Sandoval M, Storz G. 2011. The Escherichia coli MntR miniregulon includes genes encoding a small protein and an efflux pump required for manganese homeostasis. J. Bacteriol. 193:5887-97
    • (2011) J. Bacteriol , vol.193 , pp. 5887-5897
    • Waters, L.S.1    Sandoval, M.2    Storz, G.3
  • 79
    • 50149103524 scopus 로고    scopus 로고
    • The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins
    • Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, et al. 2008. The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. Proc. Natl. Acad. Sci. USA 105:11927-32
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11927-11932
    • Gaballa, A.1    Antelmann, H.2    Aguilar, C.3    Khakh, S.K.4    Song, K.B.5
  • 80
    • 0027218065 scopus 로고
    • Metalloregulation in Bacillus subtilis: Isolation and characterization of two genes differentially repressed by metal ions
    • Chen L, JamesLP, Helmann JD. 1993. Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions. J. Bacteriol. 175:5428-37
    • (1993) J. Bacteriol , vol.175 , pp. 5428-5437
    • Chen, L.1    James, L.P.2    Helmann, J.D.3
  • 81
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis fur regulon and the iron starvation stimulon
    • Baichoo N, Wang T, Ye R, Helmann JD. 2002. Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol. Microbiol. 45:1613-29
    • (2002) Mol. Microbiol , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 82
    • 84861368192 scopus 로고    scopus 로고
    • The FsrA sRNA and FbpB proteinmediate the iron-dependent induction of the Bacillus subtilis lutABC iron-sulfur-containing oxidases
    • SmaldoneGT, AntelmannH,Gaballa A, Helmann JD. 2012. The FsrA sRNA and FbpB proteinmediate the iron-dependent induction of the Bacillus subtilis lutABC iron-sulfur-containing oxidases. J. Bacteriol. 194:2586-93
    • (2012) J. Bacteriol , vol.194 , pp. 2586-2593
    • Smaldone, G.T.1    Antelmann, H.2    Gaballa, A.3    Helmann, J.D.4
  • 83
    • 79959421469 scopus 로고    scopus 로고
    • Identification of prokaryotic small proteins using a comparative genomic approach
    • Samayoa J, Yildiz FH, Karplus K. 2011. Identification of prokaryotic small proteins using a comparative genomic approach. Bioinformatics 27:1756-71
    • (2011) Bioinformatics , vol.27 , pp. 1756-1771
    • Samayoa, J.1    Yildiz, F.H.2    Karplus, K.3
  • 85
    • 0035424711 scopus 로고    scopus 로고
    • On the total number of genes and their length distribution in complete microbial genomes
    • Skovgaard M, Jensen LJ, Brunak S, Ussery D, Krogh A. 2001. On the total number of genes and their length distribution in complete microbial genomes. Trends Genet. 17:425-28
    • (2001) Trends Genet , vol.17 , pp. 425-428
    • Skovgaard, M.1    Jensen, L.J.2    Brunak, S.3    Ussery, D.4    Krogh, A.5
  • 86
    • 84860231100 scopus 로고    scopus 로고
    • The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria
    • Li GW, Oh E,Weissman JS. 2012. The anti-Shine-Dalgarno sequence drives translational pausing and codon choice in bacteria. Nature 484:538-41
    • (2012) Nature , vol.484 , pp. 538-541
    • Li, G.W.1    Oh, E.2    Weissman, J.S.3
  • 87
    • 78650513756 scopus 로고    scopus 로고
    • Identification of a chloroform-soluble membrane miniprotein in Escherichia coli and its homolog in Salmonella typhimurium
    • Guan Z, Wang X, Raetz CRH. 2011. Identification of a chloroform-soluble membrane miniprotein in Escherichia coli and its homolog in Salmonella typhimurium. Anal. Biochem. 409:284-89
    • (2011) Anal. Biochem , vol.409 , pp. 284-289
    • Guan, Z.1    Wang, X.2    Crh, R.3
  • 88
    • 84885442739 scopus 로고    scopus 로고
    • Deciphering the interplay between two independent functions of the small RNA regulator SgrS in Salmonella
    • Balasubramanian D, Vanderpool CK. 2013. Deciphering the interplay between two independent functions of the small RNA regulator SgrS in Salmonella. J. Bacteriol. 195:4620-30
    • (2013) J. Bacteriol , vol.195 , pp. 4620-4630
    • Balasubramanian, D.1    Vanderpool, C.K.2
  • 89
    • 80053019485 scopus 로고    scopus 로고
    • Regulation by small RNAs in bacteria: Expanding frontiers
    • Storz G, Vogel J, Wassarman KM. 2011. Regulation by small RNAs in bacteria: expanding frontiers. Mol. Cell 43:880-91
    • (2011) Mol. Cell , vol.43 , pp. 880-891
    • Storz, G.1    Vogel, J.2    Wassarman, K.M.3
  • 90
    • 77957971178 scopus 로고    scopus 로고
    • Basis of virulence in community-Associated methicillin-resistant Staphylococcus aureus
    • Otto M. 2010. Basis of virulence in community-Associated methicillin-resistant Staphylococcus aureus. Annu. Rev. Microbiol. 64:143-62
    • (2010) Annu. Rev. Microbiol , vol.64 , pp. 143-162
    • Otto, M.1
  • 91
    • 77951619556 scopus 로고    scopus 로고
    • Abundance of type i toxinantitoxin systems in bacteria: Searches for new candidates and discovery of novel families
    • Fozo EM,Makarova KS, Shabalina SA, YutinN, Koonin EV, Storz G. 2010. Abundance of type I toxinantitoxin systems in bacteria: searches for new candidates and discovery of novel families. Nucleic Acids Res. 38:3743-59
    • (2010) Nucleic Acids Res , vol.38 , pp. 3743-3759
    • Fozo, E.M.1    Makarova, K.S.2    Shabalina, S.A.3    Yutin, N.4    Koonin, E.V.5    Storz, G.6
  • 92
    • 84883278830 scopus 로고    scopus 로고
    • Plasmid-encoded ComI inhibits competence in the ancestral strain of Bacillus subtilis
    • Konkol MA, Blair KM, Kearns DB. 2013. Plasmid-encoded ComI inhibits competence in the ancestral strain of Bacillus subtilis. J. Bacteriol. 195:4085-93
    • (2013) J. Bacteriol , vol.195 , pp. 4085-4093
    • Konkol, M.A.1    Blair, K.M.2    Kearns, D.B.3
  • 94
    • 58149492417 scopus 로고    scopus 로고
    • Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery
    • Karimova G, Robichon C, Ladant D. 2009. Characterization of YmgF, a 72-residue inner membrane protein that associates with the Escherichia coli cell division machinery. J. Bacteriol. 191:333-46
    • (2009) J. Bacteriol , vol.191 , pp. 333-346
    • Karimova, G.1    Robichon, C.2    Ladant, D.3
  • 95
    • 36749059574 scopus 로고    scopus 로고
    • B1500, a small membrane protein, connects the two-component systems EvgS/EvgA and PhoQ/PhoP in Escherichia coli
    • Eguchi Y, Itou J, Yamane M, Demizu R, Yamato F, et al. 2007. B1500, a small membrane protein, connects the two-component systems EvgS/EvgA and PhoQ/PhoP in Escherichia coli. Proc. Natl. Acad. Sci. USA 104:18712-17
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18712-18717
    • Eguchi, Y.1    Itou, J.2    Yamane, M.3    Demizu, R.4    Yamato, F.5
  • 96
    • 36749071555 scopus 로고    scopus 로고
    • Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist
    • Törnroth-Horsefield S, Gourdon P, Horsefield R, Brive L, Yamamoto N, et al. 2007. Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist. Structure 15:1663-73
    • (2007) Structure , vol.15 , pp. 1663-1673
    • Törnroth-Horsefield, S.1    Gourdon, P.2    Horsefield, R.3    Brive, L.4    Yamamoto, N.5
  • 97
  • 98
    • 80052782538 scopus 로고    scopus 로고
    • Membrane localization of small proteins in Escherichia coli
    • Fontaine F, Fuchs RT, Storz G. 2011. Membrane localization of small proteins in Escherichia coli. J. Biol. Chem. 286:32464-74
    • (2011) J. Biol. Chem , vol.286 , pp. 32464-32474
    • Fontaine, F.1    Fuchs, R.T.2    Storz, G.3
  • 99
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K, Dalbey RE. 2008. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat. Rev. Microbiol. 6:234-44
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 100
    • 70449700233 scopus 로고    scopus 로고
    • Homologs of the small RNA SgrS are broadly distributed in enteric bacteria but have diverged in size and sequence
    • Horler RS, Vanderpool CK. 2009. Homologs of the small RNA SgrS are broadly distributed in enteric bacteria but have diverged in size and sequence. Nucleic Acids Res. 37:5465-76
    • (2009) Nucleic Acids Res , vol.37 , pp. 5465-5476
    • Horler, R.S.1    Vanderpool, C.K.2
  • 102
    • 84894380391 scopus 로고    scopus 로고
    • Emerging evidence for functional peptides encoded by small open reading frames
    • Andrews SJ, Rothnagel JA. 2014. Emerging evidence for functional peptides encoded by small open reading frames. Nat. Rev. Genet. 15:193-204
    • (2014) Nat. Rev. Genet , vol.15 , pp. 193-204
    • Andrews, S.J.1    Rothnagel, J.A.2
  • 104
    • 34447573973 scopus 로고    scopus 로고
    • Small peptide regulators of actin-based cell morphogenesis encoded by a polycistronic mRNA
    • Kondo T, Hashimoto Y, Kato K, Inagaki S, Hayashi S, Kageyama Y. 2007. Small peptide regulators of actin-based cell morphogenesis encoded by a polycistronic mRNA. Nat. Cell Biol. 9:660-65
    • (2007) Nat. Cell Biol , vol.9 , pp. 660-665
    • Kondo, T.1    Hashimoto, Y.2    Kato, K.3    Inagaki, S.4    Hayashi, S.5    Kageyama, Y.6
  • 105
    • 34249021370 scopus 로고    scopus 로고
    • Peptides encoded by short ORFs control development and define a new eukaryotic gene family
    • Galindo MI, Pueyo JI, Fouix S, Bishop SA, Couso JP. 2007. Peptides encoded by short ORFs control development and define a new eukaryotic gene family. PLoS Biol. 5:e106
    • (2007) PLoS Biol , vol.5
    • Galindo, M.I.1    Pueyo, J.I.2    Fouix, S.3    Bishop, S.A.4    Couso, J.P.5
  • 106
    • 84883487014 scopus 로고    scopus 로고
    • Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames
    • Magny EG, Pueyo JI, Pearl FM, Cespedes MA, Niven JE, et al. 2013. Conserved regulation of cardiac calcium uptake by peptides encoded in small open reading frames. Science 341:1116-20
    • (2013) Science , vol.341 , pp. 1116-1120
    • Magny, E.G.1    Pueyo, J.I.2    Pearl, F.M.3    Cespedes, M.A.4    Niven, J.E.5
  • 107
    • 77954786287 scopus 로고    scopus 로고
    • Small peptides switch the transcriptional activity of Shavenbaby during Drosophila embryogenesis
    • Kondo T, Plaza S, Zanet J, Benrabah E, Valenti P, et al. 2010. Small peptides switch the transcriptional activity of Shavenbaby during Drosophila embryogenesis. Science 329:336-39
    • (2010) Science , vol.329 , pp. 336-339
    • Kondo, T.1    Plaza, S.2    Zanet, J.3    Benrabah, E.4    Valenti, P.5


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