메뉴 건너뛰기




Volumn 10, Issue 2, 2014, Pages

Quantitative Genome-Wide Genetic Interaction Screens Reveal Global Epistatic Relationships of Protein Complexes in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

IRON SULFUR PROTEIN; CHAPERONE; MULTIPROTEIN COMPLEX;

EID: 84901742537     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1004120     Document Type: Article
Times cited : (93)

References (107)
  • 1
    • 72949098090 scopus 로고    scopus 로고
    • Systems-level approaches for identifying and analyzing genetic interaction networks in Escherichia coli and extensions to other prokaryotes
    • Babu M, Musso G, Diaz-Mejia JJ, Butland G, Greenblatt JF, et al. (2009) Systems-level approaches for identifying and analyzing genetic interaction networks in Escherichia coli and extensions to other prokaryotes. Mol Biosyst 12: 1439-1455.
    • (2009) Mol Biosyst , vol.12 , pp. 1439-1455
    • Babu, M.1    Musso, G.2    Diaz-Mejia, J.J.3    Butland, G.4    Greenblatt, J.F.5
  • 2
    • 66049143558 scopus 로고    scopus 로고
    • Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins
    • Hu P, Janga SC, Babu M, Diaz-Mejia JJ, Butland G, (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol 7: e1000096.
    • (2009) PLoS Biol , vol.7
    • Hu, P.1    Janga, S.C.2    Babu, M.3    Diaz-Mejia, J.J.4    Butland, G.5
  • 4
    • 0001291140 scopus 로고    scopus 로고
    • A powerful non-homology method for the prediction of operons in prokaryotes
    • Moreno-Hagelsieb G, Collado-Vides J, (2002) A powerful non-homology method for the prediction of operons in prokaryotes. Bioinformatics 18 Suppl 1: S329-336.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Moreno-Hagelsieb, G.1    Collado-Vides, J.2
  • 6
    • 84861125187 scopus 로고    scopus 로고
    • Genome-scale genetic manipulation methods for exploring bacterial molecular biology
    • Gagarinova A, Emili A, (2012) Genome-scale genetic manipulation methods for exploring bacterial molecular biology. Mol Biosyst 8: 1626-1638.
    • (2012) Mol Biosyst , vol.8 , pp. 1626-1638
    • Gagarinova, A.1    Emili, A.2
  • 7
    • 84866930696 scopus 로고    scopus 로고
    • Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae
    • Babu M, Vlasblom J, Pu S, Guo X, Graham C, et al. (2012) Interaction landscape of membrane-protein complexes in Saccharomyces cerevisiae. Nature 489: 585-589.
    • (2012) Nature , vol.489 , pp. 585-589
    • Babu, M.1    Vlasblom, J.2    Pu, S.3    Guo, X.4    Graham, C.5
  • 8
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin AC, Aloy P, Grandi P, Krause R, Boesche M, et al. (2006) Proteome survey reveals modularity of the yeast cell machinery. Nature pp. 631-636.
    • (2006) Nature , pp. 631-636
    • Gavin, A.C.1    Aloy, P.2    Grandi, P.3    Krause, R.4    Boesche, M.5
  • 9
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan NJ, Cagney G, Yu H, Zhong G, Guo X, et al. (2006) Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440: 637-643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5
  • 10
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G, Peregrín-Alvarez JM, Li J, Yang W, Yang X, et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-537.
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrín-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5
  • 11
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-691.
    • (2006) Genome Res , vol.16 , pp. 686-691
    • Arifuzzaman, M.1    Maeda, M.2    Itoh, A.3    Nishikata, K.4    Takita, C.5
  • 12
    • 57549088143 scopus 로고    scopus 로고
    • Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome
    • Díaz-Mejía JJ, Babu M, Emili A, (2009) Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome. FEMS Microbiol Rev 33: 66-97.
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 66-97
    • Díaz-Mejía, J.J.1    Babu, M.2    Emili, A.3
  • 14
    • 50849125711 scopus 로고    scopus 로고
    • High-throughput, quantitative analyses of genetic interactions in E. coli
    • Typas A, Nichols RJ, Siegele DA, Shales M, Collins SR, et al. (2008) High-throughput, quantitative analyses of genetic interactions in E. coli. Nat Methods 5: 781-787.
    • (2008) Nat Methods , vol.5 , pp. 781-787
    • Typas, A.1    Nichols, R.J.2    Siegele, D.A.3    Shales, M.4    Collins, S.R.5
  • 15
    • 70349611730 scopus 로고    scopus 로고
    • Tn-seq: high-throughput parallel sequencing for fitness and genetic interaction studies in microorganisms
    • van Opijnen T, Bodi KL, Camilli A, (2009) Tn-seq: high-throughput parallel sequencing for fitness and genetic interaction studies in microorganisms. Nat Methods 6: 767-772.
    • (2009) Nat Methods , vol.6 , pp. 767-772
    • van Opijnen, T.1    Bodi, K.L.2    Camilli, A.3
  • 16
    • 81755177857 scopus 로고    scopus 로고
    • Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways
    • Babu M, Díaz-Mejía JJ, Vlasblom J, Gagarinova A, Phanse S, et al. (2011) Genetic interaction maps in Escherichia coli reveal functional crosstalk among cell envelope biogenesis pathways. PLoS Genet 7: e1002377.
    • (2011) PLoS Genet , vol.7
    • Babu, M.1    Díaz-Mejía, J.J.2    Vlasblom, J.3    Gagarinova, A.4    Phanse, S.5
  • 17
    • 0742305866 scopus 로고    scopus 로고
    • Network biology: understanding the cell's functional organization
    • Barabasi AL, Oltvai ZN, (2004) Network biology: understanding the cell's functional organization. Nat Rev Genet 5: 101-113.
    • (2004) Nat Rev Genet , vol.5 , pp. 101-113
    • Barabasi, A.L.1    Oltvai, Z.N.2
  • 18
  • 19
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 2006
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5
  • 20
    • 43249117094 scopus 로고    scopus 로고
    • Functional maps of protein complexes from quantitative genetic interaction data
    • Bandyopadhyay S, Kelley R, Krogan NJ, Ideker T, (2008) Functional maps of protein complexes from quantitative genetic interaction data. PLoS Comput Biol 4: e1000065.
    • (2008) PLoS Comput Biol , vol.4
    • Bandyopadhyay, S.1    Kelley, R.2    Krogan, N.J.3    Ideker, T.4
  • 21
    • 77953236579 scopus 로고    scopus 로고
    • Quantitative genetic interactions reveal biological modularity
    • Beltrao P, Cagney G, Krogan NJ, (2010) Quantitative genetic interactions reveal biological modularity. Cell 141: 739-745.
    • (2010) Cell , vol.141 , pp. 739-745
    • Beltrao, P.1    Cagney, G.2    Krogan, N.J.3
  • 22
    • 34249041230 scopus 로고    scopus 로고
    • Exploring genetic interactions and networks with yeast
    • Boone C, Bussey H, Andrews BJ, (2007) Exploring genetic interactions and networks with yeast. Nat Rev Genet 8: 437-449.
    • (2007) Nat Rev Genet , vol.8 , pp. 437-449
    • Boone, C.1    Bussey, H.2    Andrews, B.J.3
  • 23
    • 47349120555 scopus 로고    scopus 로고
    • From E-MAPs to module maps: dissecting quantitative genetic interactions using physical interactions
    • Ulitsky I, Shlomi T, Kupiec M, Shamir R, (2008) From E-MAPs to module maps: dissecting quantitative genetic interactions using physical interactions. Mol Syst Biol 4: 209.
    • (2008) Mol Syst Biol , vol.4 , pp. 209
    • Ulitsky, I.1    Shlomi, T.2    Kupiec, M.3    Shamir, R.4
  • 25
    • 33747367151 scopus 로고    scopus 로고
    • A strategy for extracting and analyzing large-scale quantitative epistatic interaction data
    • Collins SR, Schuldiner M, Krogan NJ, Weissman JS, (2006) A strategy for extracting and analyzing large-scale quantitative epistatic interaction data. Genome Biol 7: R63.
    • (2006) Genome Biol , vol.7
    • Collins, S.R.1    Schuldiner, M.2    Krogan, N.J.3    Weissman, J.S.4
  • 26
    • 78649705725 scopus 로고    scopus 로고
    • Quantitative analysis of fitness and genetic interactions in yeast on a genome scale
    • Baryshnikova A, Costanzo M, Kim Y, Ding H, Koh J, et al. (2010) Quantitative analysis of fitness and genetic interactions in yeast on a genome scale. Nat Methods 7: 1017-1024.
    • (2010) Nat Methods , vol.7 , pp. 1017-1024
    • Baryshnikova, A.1    Costanzo, M.2    Kim, Y.3    Ding, H.4    Koh, J.5
  • 27
    • 26844489762 scopus 로고    scopus 로고
    • Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile
    • Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123: 507-519.
    • (2005) Cell , vol.123 , pp. 507-519
    • Schuldiner, M.1    Collins, S.R.2    Thompson, N.J.3    Denic, V.4    Bhamidipati, A.5
  • 31
    • 80051558597 scopus 로고    scopus 로고
    • Putting genetic interactions in context through a global modular decomposition
    • Bellay J, Atluri G, Sing TL, Toufighi K, Costanzo M, et al. (2011) Putting genetic interactions in context through a global modular decomposition. Genome Res 21: 1375-1387.
    • (2011) Genome Res , vol.21 , pp. 1375-1387
    • Bellay, J.1    Atluri, G.2    Sing, T.L.3    Toufighi, K.4    Costanzo, M.5
  • 32
    • 34147217542 scopus 로고    scopus 로고
    • Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map
    • Collins SR, Miller KM, Maas NL, Roguev A, Fillingham J, et al. (2007) Functional dissection of protein complexes involved in yeast chromosome biology using a genetic interaction map. Nature 446: 806-810.
    • (2007) Nature , vol.446 , pp. 806-810
    • Collins, S.R.1    Miller, K.M.2    Maas, N.L.3    Roguev, A.4    Fillingham, J.5
  • 33
    • 27144434505 scopus 로고    scopus 로고
    • The synthetic genetic interaction spectrum of essential genes
    • Davierwala AP, Haynes J, Li Z, Brost RL, Robinson MD, et al. (2005) The synthetic genetic interaction spectrum of essential genes. Nat Genet 37: 1147-1152.
    • (2005) Nat Genet , vol.37 , pp. 1147-1152
    • Davierwala, A.P.1    Haynes, J.2    Li, Z.3    Brost, R.L.4    Robinson, M.D.5
  • 34
    • 56849094282 scopus 로고    scopus 로고
    • A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing
    • Wilmes GM, Bergkessel M, Bandyopadhyay S, Shales M, Braberg H, et al. (2008) A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing. Mol Cell 32: 735-746.
    • (2008) Mol Cell , vol.32 , pp. 735-746
    • Wilmes, G.M.1    Bergkessel, M.2    Bandyopadhyay, S.3    Shales, M.4    Braberg, H.5
  • 35
    • 0029034167 scopus 로고
    • A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli
    • Ueguchi C, Shiozawa T, Kakeda M, Yamada H, Mizuno T, (1995) A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J Bacteriol 177: 3894-3896.
    • (1995) J Bacteriol , vol.177 , pp. 3894-3896
    • Ueguchi, C.1    Shiozawa, T.2    Kakeda, M.3    Yamada, H.4    Mizuno, T.5
  • 36
    • 0030890705 scopus 로고    scopus 로고
    • recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli
    • Courcelle J, Carswell-Crumpton C, Hanawalt PC, (1997) recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli. Proc Natl Acad Sci U S A 94: 3714-3719.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3714-3719
    • Courcelle, J.1    Carswell-Crumpton, C.2    Hanawalt, P.C.3
  • 37
    • 0025770263 scopus 로고
    • Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease
    • Chenault SS, Earhart CF, (1991) Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease. Mol Microbiol 5: 1405-1413.
    • (1991) Mol Microbiol , vol.5 , pp. 1405-1413
    • Chenault, S.S.1    Earhart, C.F.2
  • 38
    • 0025915699 scopus 로고
    • Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli
    • Shea CM, McIntosh MA, (1991) Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli. Mol Microbiol 5: 1415-1428.
    • (1991) Mol Microbiol , vol.5 , pp. 1415-1428
    • Shea, C.M.1    McIntosh, M.A.2
  • 39
    • 84856740569 scopus 로고    scopus 로고
    • Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution
    • Orchard SS, Rostron JE, Segall AM, (2012) Escherichia coli enterobactin synthesis and uptake mutants are hypersensitive to an antimicrobial peptide that limits the availability of iron in addition to blocking Holliday junction resolution. Microbiology 158: 547-559.
    • (2012) Microbiology , vol.158 , pp. 547-559
    • Orchard, S.S.1    Rostron, J.E.2    Segall, A.M.3
  • 40
    • 38549134505 scopus 로고    scopus 로고
    • Many Microbe Microarrays Database: uniformly normalized Affymetrix compendia with structured experimental metadata
    • Faith JJ, Driscoll ME, Fusaro VA, Cosgrove EJ, Hayete B, et al. (2008) Many Microbe Microarrays Database: uniformly normalized Affymetrix compendia with structured experimental metadata. Nucleic Acids Res 36: D866-870.
    • (2008) Nucleic Acids Res , vol.36
    • Faith, J.J.1    Driscoll, M.E.2    Fusaro, V.A.3    Cosgrove, E.J.4    Hayete, B.5
  • 43
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi Y, Shigi N, Kato J, Nishimura A, Suzuki T, (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell 21: 97-108.
    • (2006) Mol Cell , vol.21 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 47
    • 33645239646 scopus 로고    scopus 로고
    • Interplay between replication and recombination in Escherichia coli: impact of the alternative DNA polymerases
    • Delmas S, Matic I, (2006) Interplay between replication and recombination in Escherichia coli: impact of the alternative DNA polymerases. Proc Natl Acad Sci U S A 103: 4564-4569.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4564-4569
    • Delmas, S.1    Matic, I.2
  • 48
    • 80053905923 scopus 로고    scopus 로고
    • The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli
    • Dahl JU, Urban A, Bolte A, Sriyabhaya P, Donahue JL, et al. (2011) The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J Biol Chem 286: 35801-35812.
    • (2011) J Biol Chem , vol.286 , pp. 35801-35812
    • Dahl, J.U.1    Urban, A.2    Bolte, A.3    Sriyabhaya, P.4    Donahue, J.L.5
  • 49
    • 33749337533 scopus 로고    scopus 로고
    • MoxR AAA+ ATPases: a novel family of molecular chaperones
    • Snider J, Houry WA, (2006) MoxR AAA+ ATPases: a novel family of molecular chaperones? J Struct Biol 156: 200-209.
    • (2006) J Struct Biol , vol.156 , pp. 200-209
    • Snider, J.1    Houry, W.A.2
  • 50
    • 75849120863 scopus 로고    scopus 로고
    • Electro-Fenton process and related electrochemical technologies based on Fenton's reaction chemistry
    • Brillas E, Sires I, Oturan MA, (2009) Electro-Fenton process and related electrochemical technologies based on Fenton's reaction chemistry. Chem Rev 109: 6570-6631.
    • (2009) Chem Rev , vol.109 , pp. 6570-6631
    • Brillas, E.1    Sires, I.2    Oturan, M.A.3
  • 51
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman O, Outten FW, Imlay JA, (2004) Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem 279: 44590-44599.
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 52
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski MA, Dwyer DJ, Hayete B, Lawrence CA, Collins JJ, (2007) A common mechanism of cellular death induced by bactericidal antibiotics. Cell 130: 797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 53
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz CJ, Djaman O, Imlay JA, Kiley PJ, (2000) The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli. Proc Natl Acad Sci U S A 97: 9009-9014.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 54
    • 84879615674 scopus 로고    scopus 로고
    • Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway
    • Ezraty B, Vergnes A, Banzhaf M, Duverger Y, Huguenot A, et al. (2013) Fe-S cluster biosynthesis controls uptake of aminoglycosides in a ROS-less death pathway. Science 340: 1583-1587.
    • (2013) Science , vol.340 , pp. 1583-1587
    • Ezraty, B.1    Vergnes, A.2    Banzhaf, M.3    Duverger, Y.4    Huguenot, A.5
  • 55
    • 0032725568 scopus 로고    scopus 로고
    • Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli
    • Takahashi Y, Nakamura M, (1999) Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli. J Biochem 126: 917-926.
    • (1999) J Biochem , vol.126 , pp. 917-926
    • Takahashi, Y.1    Nakamura, M.2
  • 56
    • 0036271841 scopus 로고    scopus 로고
    • Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo
    • Wooff E, Michell SL, Gordon SV, Chambers MA, Bardarov S, et al. (2002) Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. Mol Microbiol 43: 653-663.
    • (2002) Mol Microbiol , vol.43 , pp. 653-663
    • Wooff, E.1    Michell, S.L.2    Gordon, S.V.3    Chambers, M.A.4    Bardarov, S.5
  • 58
    • 0036230993 scopus 로고    scopus 로고
    • The switch from inorganic to organic sulphur assimilation in Escherichia coli: adenosine 5′-phosphosulphate (APS) as a signalling molecule for sulphate excess
    • Bykowski T, van der Ploeg JR, Iwanicka-Nowicka R, Hryniewicz MM, (2002) The switch from inorganic to organic sulphur assimilation in Escherichia coli: adenosine 5′-phosphosulphate (APS) as a signalling molecule for sulphate excess. Mol Microbiol 43: 1347-1358.
    • (2002) Mol Microbiol , vol.43 , pp. 1347-1358
    • Bykowski, T.1    van der Ploeg, J.R.2    Iwanicka-Nowicka, R.3    Hryniewicz, M.M.4
  • 59
    • 0034015228 scopus 로고    scopus 로고
    • Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems
    • Eichhorn E, van der Ploeg JR, Leisinger T, (2000) Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems. J Bacteriol 182: 2687-2695.
    • (2000) J Bacteriol , vol.182 , pp. 2687-2695
    • Eichhorn, E.1    van der Ploeg, J.R.2    Leisinger, T.3
  • 60
    • 0034098682 scopus 로고    scopus 로고
    • Growth phase-coupled changes of the ribosome profile in natural isolates and laboratory strains of Escherichia coli
    • Wada A, Mikkola R, Kurland CG, Ishihama A, (2000) Growth phase-coupled changes of the ribosome profile in natural isolates and laboratory strains of Escherichia coli. J Bacteriol 182: 2893-2899.
    • (2000) J Bacteriol , vol.182 , pp. 2893-2899
    • Wada, A.1    Mikkola, R.2    Kurland, C.G.3    Ishihama, A.4
  • 61
    • 0026703121 scopus 로고
    • A ribosomal ambiguity mutation in the 530 loop of E. coli 16S rRNA
    • O'Connor M, Goringer HU, Dahlberg AE, (1992) A ribosomal ambiguity mutation in the 530 loop of E. coli 16S rRNA. Nucleic Acids Res 20: 4221-4227.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4221-4227
    • O'Connor, M.1    Goringer, H.U.2    Dahlberg, A.E.3
  • 62
    • 79952996835 scopus 로고    scopus 로고
    • Understanding ribosome assembly: the structure of in vivo assembled immature 30S subunits revealed by cryo-electron microscopy
    • Jomaa A, Stewart G, Martin-Benito J, Zielke R, Campbell TL, et al. (2011) Understanding ribosome assembly: the structure of in vivo assembled immature 30S subunits revealed by cryo-electron microscopy. RNA 17: 697-709.
    • (2011) RNA , vol.17 , pp. 697-709
    • Jomaa, A.1    Stewart, G.2    Martin-Benito, J.3    Zielke, R.4    Campbell, T.L.5
  • 63
    • 84878025011 scopus 로고    scopus 로고
    • Escherichia coli rimM and yjeQ null strains accumulate immature 30S subunits of similar structure and protein complement
    • Leong V, Kent M, Jomaa A, Ortega J, (2013) Escherichia coli rimM and yjeQ null strains accumulate immature 30S subunits of similar structure and protein complement. RNA 19: 789-802.
    • (2013) RNA , vol.19 , pp. 789-802
    • Leong, V.1    Kent, M.2    Jomaa, A.3    Ortega, J.4
  • 64
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M, (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16: 574-581.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 65
    • 1642351870 scopus 로고    scopus 로고
    • Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells
    • Wong P, Houry WA, (2004) Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells. J Struct Biol 146: 79-89.
    • (2004) J Struct Biol , vol.146 , pp. 79-89
    • Wong, P.1    Houry, W.A.2
  • 66
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell
    • Gong Y, Kakihara Y, Krogan N, Greenblatt J, Emili A, et al. (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5: 275.
    • (2009) Mol Syst Biol , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5
  • 67
    • 84860600452 scopus 로고    scopus 로고
    • Physical map and dynamics of the chaperone network in Escherichia coli
    • Kumar M, Sourjik V, (2012) Physical map and dynamics of the chaperone network in Escherichia coli. Mol Microbiol 84: 736-747.
    • (2012) Mol Microbiol , vol.84 , pp. 736-747
    • Kumar, M.1    Sourjik, V.2
  • 68
    • 84855195754 scopus 로고    scopus 로고
    • ClpXP, an ATP-powered unfolding and protein-degradation machine
    • Baker TA, Sauer RT, (2012) ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta 1823: 15-28.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 15-28
    • Baker, T.A.1    Sauer, R.T.2
  • 69
    • 79959389010 scopus 로고    scopus 로고
    • AAA+ proteases: ATP-fueled machines of protein destruction
    • Sauer RT, Baker TA, (2011) AAA+ proteases: ATP-fueled machines of protein destruction. Annu Rev Biochem 80: 587-612.
    • (2011) Annu Rev Biochem , vol.80 , pp. 587-612
    • Sauer, R.T.1    Baker, T.A.2
  • 70
    • 0035957317 scopus 로고    scopus 로고
    • ClpA mediates directional translocation of substrate proteins into the ClpP protease
    • Reid BG, Fenton WA, Horwich AL, Weber-Ban EU, (2001) ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc Natl Acad Sci U S A 98: 3768-3772.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3768-3772
    • Reid, B.G.1    Fenton, W.A.2    Horwich, A.L.3    Weber-Ban, E.U.4
  • 71
    • 58549098512 scopus 로고    scopus 로고
    • Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
    • Ratajczak E, Zietkiewicz S, Liberek K, (2009) Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J Mol Biol 386: 178-189.
    • (2009) J Mol Biol , vol.386 , pp. 178-189
    • Ratajczak, E.1    Zietkiewicz, S.2    Liberek, K.3
  • 72
    • 84856071924 scopus 로고    scopus 로고
    • Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization
    • Strozecka J, Chrusciel E, Gorna E, Szymanska A, Zietkiewicz S, et al. (2012) Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization. J Biol Chem 287: 2843-2853.
    • (2012) J Biol Chem , vol.287 , pp. 2843-2853
    • Strozecka, J.1    Chrusciel, E.2    Gorna, E.3    Szymanska, A.4    Zietkiewicz, S.5
  • 73
    • 0035800729 scopus 로고    scopus 로고
    • Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis
    • Singh SK, Rozycki J, Ortega J, Ishikawa T, Lo J, et al. (2001) Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J Biol Chem 276: 29420-29429.
    • (2001) J Biol Chem , vol.276 , pp. 29420-29429
    • Singh, S.K.1    Rozycki, J.2    Ortega, J.3    Ishikawa, T.4    Lo, J.5
  • 74
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo
    • Thomas JG, Baneyx F, (1998) Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo. J Bacteriol 180: 5165-5172.
    • (1998) J Bacteriol , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 75
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases
    • Kirstein J, Moliere N, Dougan DA, Turgay K, (2009) Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nat Rev Microbiol 7: 589-599.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 589-599
    • Kirstein, J.1    Moliere, N.2    Dougan, D.A.3    Turgay, K.4
  • 76
    • 0034081637 scopus 로고    scopus 로고
    • Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins
    • Saibil H, (2000) Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins. Curr Opin Struct Biol 10: 251-258.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 251-258
    • Saibil, H.1
  • 77
    • 79957730170 scopus 로고    scopus 로고
    • Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
    • Genest O, Hoskins JR, Camberg JL, Doyle SM, Wickner S, (2011) Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc Natl Acad Sci U S A 108: 8206-8211.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 8206-8211
    • Genest, O.1    Hoskins, J.R.2    Camberg, J.L.3    Doyle, S.M.4    Wickner, S.5
  • 78
    • 34548742517 scopus 로고    scopus 로고
    • Identification of functional modules using network topology and high-throughput data
    • Ulitsky I, Shamir R, (2007) Identification of functional modules using network topology and high-throughput data. BMC Syst Biol 1: 8.
    • (2007) BMC Syst Biol , vol.1 , pp. 8
    • Ulitsky, I.1    Shamir, R.2
  • 79
    • 77955427058 scopus 로고    scopus 로고
    • The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions
    • Arenas FA, Diaz WA, Leal CA, Perez-Donoso JM, Imlay JA, et al. (2010) The Escherichia coli btuE gene, encodes a glutathione peroxidase that is induced under oxidative stress conditions. Biochem Biophys Res Commun 398: 690-694.
    • (2010) Biochem Biophys Res Commun , vol.398 , pp. 690-694
    • Arenas, F.A.1    Diaz, W.A.2    Leal, C.A.3    Perez-Donoso, J.M.4    Imlay, J.A.5
  • 81
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • Py B, Moreau PL, Barras F, (2011) Fe-S clusters, fragile sentinels of the cell. Curr Opin Microbiol 14: 218-223.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 82
    • 29344433036 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery
    • Kitaoka S, Wada K, Hasegawa Y, Minami Y, Fukuyama K, et al. (2006) Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery. FEBS Lett 580: 137-143.
    • (2006) FEBS Lett , vol.580 , pp. 137-143
    • Kitaoka, S.1    Wada, K.2    Hasegawa, Y.3    Minami, Y.4    Fukuyama, K.5
  • 83
    • 0035170767 scopus 로고    scopus 로고
    • Identification of the ABC protein SapD as the subunit that confers ATP dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli K-12
    • Harms C, Domoto Y, Celik C, Rahe E, Stumpe S, et al. (2001) Identification of the ABC protein SapD as the subunit that confers ATP dependence to the K+-uptake systems Trk(H) and Trk(G) from Escherichia coli K-12. Microbiology 147: 2991-3003.
    • (2001) Microbiology , vol.147 , pp. 2991-3003
    • Harms, C.1    Domoto, Y.2    Celik, C.3    Rahe, E.4    Stumpe, S.5
  • 84
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology
    • Joly N, Engl C, Jovanovic G, Huvet M, Toni T, et al. (2010) Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol Rev 34: 797-827.
    • (2010) FEMS Microbiol Rev , vol.34 , pp. 797-827
    • Joly, N.1    Engl, C.2    Jovanovic, G.3    Huvet, M.4    Toni, T.5
  • 85
    • 40349098615 scopus 로고    scopus 로고
    • Nucleotide biosynthesis is critical for growth of bacteria in human blood
    • Samant S, Lee H, Ghassemi M, Chen J, Cook JL, et al. (2008) Nucleotide biosynthesis is critical for growth of bacteria in human blood. PLoS Pathog 4: e37.
    • (2008) PLoS Pathog , vol.4
    • Samant, S.1    Lee, H.2    Ghassemi, M.3    Chen, J.4    Cook, J.L.5
  • 86
    • 0041318860 scopus 로고    scopus 로고
    • Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
    • Bertero MG, Rothery RA, Palak M, Hou C, Lim D, et al. (2003) Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A. Nat Struct Biol 10: 681-687.
    • (2003) Nat Struct Biol , vol.10 , pp. 681-687
    • Bertero, M.G.1    Rothery, R.A.2    Palak, M.3    Hou, C.4    Lim, D.5
  • 87
    • 84874734350 scopus 로고    scopus 로고
    • Global Stress Response in a Prokaryotic Model of DJ-1-Associated Parkinsonism
    • Messaoudi N, Gautier V, Kthiri F, Lelandais G, Mihoub M, et al. (2013) Global Stress Response in a Prokaryotic Model of DJ-1-Associated Parkinsonism. J Bacteriol 195: 1167-1178.
    • (2013) J Bacteriol , vol.195 , pp. 1167-1178
    • Messaoudi, N.1    Gautier, V.2    Kthiri, F.3    Lelandais, G.4    Mihoub, M.5
  • 88
    • 0032469437 scopus 로고    scopus 로고
    • Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask
    • Wang J, Hartling JA, Flanagan JM, (1998) Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J Struct Biol 124: 151-163.
    • (1998) J Struct Biol , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 89
    • 84861203603 scopus 로고    scopus 로고
    • eggNOG v3.0: orthologous groups covering 1133 organisms at 41 different taxonomic ranges
    • Powell S, Szklarczyk D, Trachana K, Roth A, Kuhn M, et al. (2012) eggNOG v3.0: orthologous groups covering 1133 organisms at 41 different taxonomic ranges. Nucleic Acids Res 40: D284-289.
    • (2012) Nucleic Acids Res , vol.40
    • Powell, S.1    Szklarczyk, D.2    Trachana, K.3    Roth, A.4    Kuhn, M.5
  • 90
    • 0025362790 scopus 로고
    • Roles of the two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behavior
    • Clark RL, Neidhardt FC, (1990) Roles of the two lysyl-tRNA synthetases of Escherichia coli: analysis of nucleotide sequences and mutant behavior. J Bacteriol 172: 3237-3243.
    • (1990) J Bacteriol , vol.172 , pp. 3237-3243
    • Clark, R.L.1    Neidhardt, F.C.2
  • 91
    • 0029643954 scopus 로고
    • The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli
    • Onesti S, Miller AD, Brick P, (1995) The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli. Structure 3: 163-176.
    • (1995) Structure , vol.3 , pp. 163-176
    • Onesti, S.1    Miller, A.D.2    Brick, P.3
  • 92
    • 0034444676 scopus 로고    scopus 로고
    • Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar typhimurium and Escherichia coli
    • Chilcott GS, Hughes KT, (2000) Coupling of flagellar gene expression to flagellar assembly in Salmonella enterica serovar typhimurium and Escherichia coli. Microbiol Mol Biol Rev 64: 694-708.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 694-708
    • Chilcott, G.S.1    Hughes, K.T.2
  • 93
    • 54249107599 scopus 로고    scopus 로고
    • Conservation and rewiring of functional modules revealed by an epistasis map in fission yeast
    • Roguev A, Bandyopadhyay S, Zofall M, Zhang K, Fischer T, et al. (2008) Conservation and rewiring of functional modules revealed by an epistasis map in fission yeast. Science 322: 405-410.
    • (2008) Science , vol.322 , pp. 405-410
    • Roguev, A.1    Bandyopadhyay, S.2    Zofall, M.3    Zhang, K.4    Fischer, T.5
  • 94
    • 55949124306 scopus 로고    scopus 로고
    • Significant conservation of synthetic lethal genetic interaction networks between distantly related eukaryotes
    • Dixon SJ, Fedyshyn Y, Koh JL, Prasad TS, Chahwan C, et al. (2008) Significant conservation of synthetic lethal genetic interaction networks between distantly related eukaryotes. Proc Natl Acad Sci U S A 105: 16653-16658.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 16653-16658
    • Dixon, S.J.1    Fedyshyn, Y.2    Koh, J.L.3    Prasad, T.S.4    Chahwan, C.5
  • 95
    • 33646593180 scopus 로고    scopus 로고
    • How pathogenic bacteria evade mammalian sabotage in the battle for iron
    • Fischbach MA, Lin H, Liu DR, Walsh CT, (2006) How pathogenic bacteria evade mammalian sabotage in the battle for iron. Nat Chem Biol 2: 132-138.
    • (2006) Nat Chem Biol , vol.2 , pp. 132-138
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 96
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M, Marahiel MA, (2007) Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 71: 413-451.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 97
    • 79952467900 scopus 로고    scopus 로고
    • Thiamin (vitamin B1) biosynthesis and regulation: a rich source of antimicrobial drug targets
    • Du Q, Wang H, Xie J, (2011) Thiamin (vitamin B1) biosynthesis and regulation: a rich source of antimicrobial drug targets? Int J Biol Sci 7: 41-52.
    • (2011) Int J Biol Sci , vol.7 , pp. 41-52
    • Du, Q.1    Wang, H.2    Xie, J.3
  • 98
    • 67650729745 scopus 로고    scopus 로고
    • The structural and biochemical foundations of thiamin biosynthesis
    • Jurgenson CT, Begley TP, Ealick SE, (2009) The structural and biochemical foundations of thiamin biosynthesis. Annu Rev Biochem 78: 569-603.
    • (2009) Annu Rev Biochem , vol.78 , pp. 569-603
    • Jurgenson, C.T.1    Begley, T.P.2    Ealick, S.E.3
  • 99
    • 33644644466 scopus 로고    scopus 로고
    • Identification and analysis of evolutionarily cohesive functional modules in protein networks
    • Campillos M, von Mering C, Jensen LJ, Bork P, (2006) Identification and analysis of evolutionarily cohesive functional modules in protein networks. Genome Res 16: 374-382.
    • (2006) Genome Res , vol.16 , pp. 374-382
    • Campillos, M.1    von Mering, C.2    Jensen, L.J.3    Bork, P.4
  • 100
  • 101
    • 84861139210 scopus 로고    scopus 로고
    • DnaK functions as a central hub in the E. coli chaperone network
    • Calloni G, Chen T, Schermann SM, Chang HC, Genevaux P, et al. (2012) DnaK functions as a central hub in the E. coli chaperone network. Cell Rep 1: 251-264.
    • (2012) Cell Rep , vol.1 , pp. 251-264
    • Calloni, G.1    Chen, T.2    Schermann, S.M.3    Chang, H.C.4    Genevaux, P.5
  • 102
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong AH, Evangelista M, Parsons AB, Xu H, Bader GD, et al. (2001) Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294: 2364-2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5
  • 103
    • 84864046645 scopus 로고    scopus 로고
    • Multiple genetic interaction experiments provide complementary information useful for gene function prediction
    • Michaut M, Bader GD, (2012) Multiple genetic interaction experiments provide complementary information useful for gene function prediction. PLoS Comput Biol 8: e1002559.
    • (2012) PLoS Comput Biol , vol.8
    • Michaut, M.1    Bader, G.D.2
  • 104
    • 84866986817 scopus 로고    scopus 로고
    • Computational systems biology and in silico modeling of the human microbiome
    • Borenstein E, (2012) Computational systems biology and in silico modeling of the human microbiome. Brief Bioinform 13: 769-780.
    • (2012) Brief Bioinform , vol.13 , pp. 769-780
    • Borenstein, E.1
  • 105
    • 79952306781 scopus 로고    scopus 로고
    • Redundancy and specificity of Escherichia coli iron acquisition systems during urinary tract infection
    • Garcia EC, Brumbaugh AR, Mobley HL, (2011) Redundancy and specificity of Escherichia coli iron acquisition systems during urinary tract infection. Infect Immun 79: 1225-1235.
    • (2011) Infect Immun , vol.79 , pp. 1225-1235
    • Garcia, E.C.1    Brumbaugh, A.R.2    Mobley, H.L.3
  • 106
    • 79960963391 scopus 로고    scopus 로고
    • Borrelia burgdorferi requires glycerol for maximum fitness during the tick phase of the enzootic cycle
    • Pappas CJ, Iyer R, Petzke MM, Caimano MJ, Radolf JD, et al. (2011) Borrelia burgdorferi requires glycerol for maximum fitness during the tick phase of the enzootic cycle. PLoS Pathog 7: e1002102.
    • (2011) PLoS Pathog , vol.7
    • Pappas, C.J.1    Iyer, R.2    Petzke, M.M.3    Caimano, M.J.4    Radolf, J.D.5
  • 107
    • 0033577789 scopus 로고    scopus 로고
    • RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA
    • Li Z, Pandit S, Deutscher MP, (1999) RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA. EMBO J 18: 2878-2885.
    • (1999) EMBO J , vol.18 , pp. 2878-2885
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.