메뉴 건너뛰기




Volumn 91, Issue 1, 2014, Pages 145-157

YciM is an essential gene required for regulation of lipopolysaccharide synthesis in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

LIPID A; LIPOPOLYSACCHARIDE; ACYL-(ACYL-CARRIER-PROTEIN)-UDP-N-ACETYLGLUCOSAMINE ACYLTRANSFERASE; ACYLTRANSFERASE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; AMIDASE; ANTIINFECTIVE AGENT; ESCHERICHIA COLI PROTEIN; FTSH PROTEIN, E COLI; MEMBRANE PROTEIN; UDP-3-O-ACYL-N-ACETYLGLUCOSAMINE DEACETYLASE; YCIM PROTEIN, E COLI;

EID: 84891154708     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12452     Document Type: Article
Times cited : (77)

References (53)
  • 1
    • 0025005224 scopus 로고
    • Genetic analysis of lipopolysaccharide core biosynthesis by Escherichia coli K-12: insertion mutagenesis of the rfa locus
    • Austin, E.A., Graves, J.F., Hite, L.A., Parker, C.T., and Schnaitman, C.A. (1990) Genetic analysis of lipopolysaccharide core biosynthesis by Escherichia coli K-12: insertion mutagenesis of the rfa locus. J Bacteriol 172: 5312-5325.
    • (1990) J Bacteriol , vol.172 , pp. 5312-5325
    • Austin, E.A.1    Graves, J.F.2    Hite, L.A.3    Parker, C.T.4    Schnaitman, C.A.5
  • 2
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knock-out mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 3
    • 0023608175 scopus 로고
    • Sequence analysis, transcriptional organization and insertional mutagenesis of the envA gene of Escherichia coli
    • Beall, B., and Lutkenhaus, J. (1987) Sequence analysis, transcriptional organization and insertional mutagenesis of the envA gene of Escherichia coli. J Bacteriol 169: 5408-5415.
    • (1987) J Bacteriol , vol.169 , pp. 5408-5415
    • Beall, B.1    Lutkenhaus, J.2
  • 4
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch, G.L., and Lassle, M. (1999) The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 21: 932-939.
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 5
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M.P., Robert, V., and Tommassen, J. (2007) Biogenesis of the Gram-negative bacterial outer membrane. Annu Rev Microbiol 61: 191-214.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 7
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: the versatile helix
    • D'Andrea, L.D., and Regan, L. (2003) TPR proteins: the versatile helix. Trends Biochem Sci 28: 655-662.
    • (2003) Trends Biochem Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 8
    • 33645085050 scopus 로고    scopus 로고
    • The C-terminal of LpxC is required for degradation by the FtsH protease
    • Führer, F., Langklotz, S., and Narberhaus, F. (2006) The C-terminal of LpxC is required for degradation by the FtsH protease. Mol Microbiol 59: 1025-1036.
    • (2006) Mol Microbiol , vol.59 , pp. 1025-1036
    • Führer, F.1    Langklotz, S.2    Narberhaus, F.3
  • 9
    • 0025220127 scopus 로고
    • A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis
    • Galloway, A., and Raetz, C.R.H. (1990) A mutant of Escherichia coli defective in the first step of endotoxin biosynthesis. J Biol Chem 265: 6394-6402.
    • (1990) J Biol Chem , vol.265 , pp. 6394-6402
    • Galloway, A.1    Raetz, C.R.H.2
  • 10
    • 0025953630 scopus 로고
    • ColE1-type vectors with fully repressible replication
    • Gil, D., and Bouche, J-P. (1991) ColE1-type vectors with fully repressible replication. Gene 105: 17-22.
    • (1991) Gene , vol.105 , pp. 17-22
    • Gil, D.1    Bouche, J.2
  • 12
    • 25844525796 scopus 로고    scopus 로고
    • Cellular functions, mechanism of action, and regulation of FtsH protease
    • Ito, K., and Akiyama, Y. (2005) Cellular functions, mechanism of action, and regulation of FtsH protease. Annu Rev Microbiol 59: 211-231.
    • (2005) Annu Rev Microbiol , vol.59 , pp. 211-231
    • Ito, K.1    Akiyama, Y.2
  • 13
    • 0018087520 scopus 로고
    • A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria
    • Karkhanis, Y.D., Zeltner, J.Y., Jackson, J.J., and Carlo, D.J. (1978) A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria. Anal Biochem 85: 595-601.
    • (1978) Anal Biochem , vol.85 , pp. 595-601
    • Karkhanis, Y.D.1    Zeltner, J.Y.2    Jackson, J.J.3    Carlo, D.J.4
  • 14
    • 55749093837 scopus 로고    scopus 로고
    • Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli
    • Katz, C., and Ron, E.Z. (2008) Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli. J Bacteriol 190: 7117-7122.
    • (2008) J Bacteriol , vol.190 , pp. 7117-7122
    • Katz, C.1    Ron, E.Z.2
  • 15
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H., etal. (2006) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12: 291-299.
    • (2006) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6
  • 16
    • 0031750745 scopus 로고    scopus 로고
    • Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12
    • Kloser, A., Laird, M., Deng, M., and Misra, R. (1998) Modulations in lipid A and phospholipid biosynthesis pathways influence outer membrane protein assembly in Escherichia coli K-12. Mol Microbiol 27: 1003-1008.
    • (1998) Mol Microbiol , vol.27 , pp. 1003-1008
    • Kloser, A.1    Laird, M.2    Deng, M.3    Misra, R.4
  • 17
    • 0029787855 scopus 로고    scopus 로고
    • asmB, a suppressor locus for assembly-defective outer-membrane proteins of E. coli, is allelic to envA (lpxC)
    • Kloser, A.W., Laird, M.W., and Misra, R. (1996) asmB, a suppressor locus for assembly-defective outer-membrane proteins of E. coli, is allelic to envA (lpxC). J Bacteriol 178: 5138-5143.
    • (1996) J Bacteriol , vol.178 , pp. 5138-5143
    • Kloser, A.W.1    Laird, M.W.2    Misra, R.3
  • 18
    • 79951634603 scopus 로고    scopus 로고
    • Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all Gram-negative bacteria
    • Langklotz, S., Schakermann, M., and Narberhaus, F. (2011) Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all Gram-negative bacteria. J Bacteriol 193: 1090-1097.
    • (2011) J Bacteriol , vol.193 , pp. 1090-1097
    • Langklotz, S.1    Schakermann, M.2    Narberhaus, F.3
  • 19
    • 84855198122 scopus 로고    scopus 로고
    • Structure and function of the bacterial AAA protease FtsH
    • Langklotz, S., Baumann, U., and Narberhaus, F. (2012) Structure and function of the bacterial AAA protease FtsH. Biochim Biophys Acta 1823: 40-48.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 40-48
    • Langklotz, S.1    Baumann, U.2    Narberhaus, F.3
  • 20
    • 0018968545 scopus 로고
    • Prokaryotic histone-like protein interacting with RNA polymerase
    • Lathe, R., Buc, H., Lecocq, J.-P., and Bautz, E.K.F. (1980) Prokaryotic histone-like protein interacting with RNA polymerase. Proc Natl Acad Sci USA 77: 3548-3552.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3548-3552
    • Lathe, R.1    Buc, H.2    Lecocq, J.-P.3    Bautz, E.K.F.4
  • 21
    • 0025088052 scopus 로고
    • Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability
    • Lerner, C.G., and Inouye, M. (1990) Low copy number plasmids for regulated low-level expression of cloned genes in Escherichia coli with blue/white insert screening capability. Nucleic Acids Res 18: 4631.
    • (1990) Nucleic Acids Res , vol.18 , pp. 4631
    • Lerner, C.G.1    Inouye, M.2
  • 23
    • 0028584330 scopus 로고
    • An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase
    • Mohan, S., Kelly, T.M., Eveland, S.S., Raetz, C.R.H., and Anderson, M.S. (1994) An Escherichia coli gene (FabZ) encoding (3R)-hydroxymyristoyl acyl carrier protein dehydrase. J Biol Chem 269: 32896-32903.
    • (1994) J Biol Chem , vol.269 , pp. 32896-32903
    • Mohan, S.1    Kelly, T.M.2    Eveland, S.S.3    Raetz, C.R.H.4    Anderson, M.S.5
  • 24
  • 25
    • 47149096184 scopus 로고    scopus 로고
    • A genome-wide approach to identify the genes involved in biofilm formation in Escherichia coli
    • Niba, E.T., Naka, Y., Nagase, M., Mori, H., and Kitakawa, M. (2007) A genome-wide approach to identify the genes involved in biofilm formation in Escherichia coli. DNA Res 14: 237-246.
    • (2007) DNA Res , vol.14 , pp. 237-246
    • Niba, E.T.1    Naka, Y.2    Nagase, M.3    Mori, H.4    Kitakawa, M.5
  • 27
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane
    • 2nd edn. Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., eds). Washington, DC: ASM press
    • Nikaido, H. (1996) Outer membrane. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn. Neidhardt, F.C., Curtiss, R., III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., etal. (eds). Washington, DC: ASM press, pp. 29-47.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 29-47
    • Nikaido, H.1
  • 28
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 29
    • 33745618956 scopus 로고    scopus 로고
    • Regulon and promoter analysis of the Escherichia coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress
    • Nonaka, G., Blankschien, M., Herman, C., Gross, C.A., and Rhodius, V.A. (2006) Regulon and promoter analysis of the Escherichia coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress. Genes Dev 20: 1776-1789.
    • (2006) Genes Dev , vol.20 , pp. 1776-1789
    • Nonaka, G.1    Blankschien, M.2    Herman, C.3    Gross, C.A.4    Rhodius, V.A.5
  • 30
    • 0014478053 scopus 로고
    • Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics
    • Normark, S., Boman, H.G., and Matsson, E. (1969) Mutant of Escherichia coli with anomalous cell division and ability to decrease episomally and chromosomally mediated resistance to ampicillin and several other antibiotics. J Bacteriol 97: 1334-1342.
    • (1969) J Bacteriol , vol.97 , pp. 1334-1342
    • Normark, S.1    Boman, H.G.2    Matsson, E.3
  • 31
    • 0345523771 scopus 로고    scopus 로고
    • Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
    • Ogura, T., Inoue, K., Tatsuta, T., Suzaki, T., Karata, K., Young, K., etal. (1999) Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli. Mol Microbiol 31: 833-844.
    • (1999) Mol Microbiol , vol.31 , pp. 833-844
    • Ogura, T.1    Inoue, K.2    Tatsuta, T.3    Suzaki, T.4    Karata, K.5    Young, K.6
  • 33
    • 0003341153 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharides: a remarkable family of bioactive macroamphiphiles
    • 2nd edn. Neidhardt, F.C., Curtiss, R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., eds). Washington, DC: ASM press
    • Raetz, C.R.H. (1996) Bacterial lipopolysaccharides: a remarkable family of bioactive macroamphiphiles. In Escherichia coli and Salmonella: Cellular and Molecular Biology, 2nd edn. Neidhardt, F.C., Curtiss, R. III, Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., etal. (eds). Washington, DC: ASM press, pp. 1035-1063.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1035-1063
    • Raetz, C.R.H.1
  • 34
    • 0025017436 scopus 로고
    • Biosynthesis and function of phospholipids in Escherichia coli
    • Raetz, C.R.H., and Dowhan, W. (1990) Biosynthesis and function of phospholipids in Escherichia coli. J Biol Chem 265: 1235-1238.
    • (1990) J Biol Chem , vol.265 , pp. 1235-1238
    • Raetz, C.R.H.1    Dowhan, W.2
  • 36
    • 33845944955 scopus 로고    scopus 로고
    • Role of FtsEX in cell division of Escherichia coli: viability of ftsEX mutants is dependent on functional SufI or high osmotic strength
    • Reddy, M. (2007) Role of FtsEX in cell division of Escherichia coli: viability of ftsEX mutants is dependent on functional SufI or high osmotic strength. J Bacteriol 189: 98-108.
    • (2007) J Bacteriol , vol.189 , pp. 98-108
    • Reddy, M.1
  • 37
    • 69249230732 scopus 로고    scopus 로고
    • Transport of lipopolysaccharide across the cell envelope: the long road of discovery
    • Ruiz, N., Kahne, D., and Silhavy, T.J. (2009) Transport of lipopolysaccharide across the cell envelope: the long road of discovery. Nat Rev Microbiol 7: 677-683.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 677-683
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 39
    • 84876189820 scopus 로고    scopus 로고
    • FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp
    • Schakermann, M., Langklotz, S., and Narberhaus, F. (2013) FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp. J Bacteriol 195: 1912-1919.
    • (2013) J Bacteriol , vol.195 , pp. 1912-1919
    • Schakermann, M.1    Langklotz, S.2    Narberhaus, F.3
  • 40
    • 0027202811 scopus 로고
    • Genetics of lipopolysaccharide biosynthesis in enteric bacteria
    • Schnaitman, C.A., and Klena, J.D. (1993) Genetics of lipopolysaccharide biosynthesis in enteric bacteria. Microbiol Rev 57: 655-682.
    • (1993) Microbiol Rev , vol.57 , pp. 655-682
    • Schnaitman, C.A.1    Klena, J.D.2
  • 41
    • 0033551778 scopus 로고    scopus 로고
    • The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5
    • Sinclair, C., Borchers, C., Parker, C., Tomer, K., Charbonneau, H., and Rossie, S. (1999) The tetratricopeptide repeat domain and a C-terminal region control the activity of Ser/Thr protein phosphatase 5. J Biol Chem 274: 23666-23672.
    • (1999) J Biol Chem , vol.274 , pp. 23666-23672
    • Sinclair, C.1    Borchers, C.2    Parker, C.3    Tomer, K.4    Charbonneau, H.5    Rossie, S.6
  • 42
    • 0029908978 scopus 로고    scopus 로고
    • Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli
    • Sorensen, P.G., Lutkenhaus, J., Young, K., Eveland, S.S., Anderson, M.S., and Raetz, C.R.H. (1996) Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. J Biol Chem 271: 25898-25905.
    • (1996) J Biol Chem , vol.271 , pp. 25898-25905
    • Sorensen, P.G.1    Lutkenhaus, J.2    Young, K.3    Eveland, S.S.4    Anderson, M.S.5    Raetz, C.R.H.6
  • 43
    • 0021746019 scopus 로고
    • Transcriptional organization within Escherichia coli cell division gene cluster: direction of transcription of cell separation gene envA
    • Sullivan, V.F., and Donachie, D. (1984) Transcriptional organization within Escherichia coli cell division gene cluster: direction of transcription of cell separation gene envA. J Bacteriol 160: 724-732.
    • (1984) J Bacteriol , vol.160 , pp. 724-732
    • Sullivan, V.F.1    Donachie, D.2
  • 45
    • 2342542372 scopus 로고    scopus 로고
    • Biosynthesis, transport, and modification of lipid A
    • Trent, M.S. (2004) Biosynthesis, transport, and modification of lipid A. Biochem Cell Biol 82: 71-86.
    • (2004) Biochem Cell Biol , vol.82 , pp. 71-86
    • Trent, M.S.1
  • 46
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. (1992) Agents that increase the permeability of the outer membrane. Microbiol Rev 56: 395-411.
    • (1992) Microbiol Rev , vol.56 , pp. 395-411
    • Vaara, M.1
  • 47
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z Ring, FtsA, FtsQ, and FtsL
    • Weiss, D.S., Chen, J.C., Ghigo, J.-M., Boyd, D., and Beckwith, J. (1999) Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z Ring, FtsA, FtsQ, and FtsL. J Bacteriol 181: 508-520.
    • (1999) J Bacteriol , vol.181 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.-M.3    Boyd, D.4    Beckwith, J.5
  • 48
    • 61449087319 scopus 로고    scopus 로고
    • Environmental pH affects transcriptional responses to cadmium toxicity in Escherichia coli K-12 (MG1655)
    • Worden, C.R., Kovak, W.K., Dorn, L.A., and Sandrin, T.R. (2009) Environmental pH affects transcriptional responses to cadmium toxicity in Escherichia coli K-12 (MG1655). FEMS Microbiol Lett 293: 58-64.
    • (2009) FEMS Microbiol Lett , vol.293 , pp. 58-64
    • Worden, C.R.1    Kovak, W.K.2    Dorn, L.A.3    Sandrin, T.R.4
  • 49
    • 0029586501 scopus 로고
    • The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis
    • Young, K., Silver, L.L., Bramhill, D., Cameron, P., Eveland, S.S., Raetz, C.R.H., etal. (1995) The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. J Biol Chem 270: 30384-30391.
    • (1995) J Biol Chem , vol.270 , pp. 30384-30391
    • Young, K.1    Silver, L.L.2    Bramhill, D.3    Cameron, P.4    Eveland, S.S.5    Raetz, C.R.H.6
  • 51
    • 33746415885 scopus 로고    scopus 로고
    • A comprehensive library of fluorescent transcriptional reporters for Escherichia coli
    • Zaslaver, A., Bren, A., Ronen, M., Itzkovitz, S., Kikoin, I., Shavit, S., etal. (2006) A comprehensive library of fluorescent transcriptional reporters for Escherichia coli. Nat Methods 3: 623-628.
    • (2006) Nat Methods , vol.3 , pp. 623-628
    • Zaslaver, A.1    Bren, A.2    Ronen, M.3    Itzkovitz, S.4    Kikoin, I.5    Shavit, S.6
  • 52
    • 84874307225 scopus 로고    scopus 로고
    • Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis
    • Zeng, D., Zhao, J., Chung, H.S., Guan, Z., Raetz, C.R.H., and Zhou, P. (2013) Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis. J Biol Chem 288: 5475-5486.
    • (2013) J Biol Chem , vol.288 , pp. 5475-5486
    • Zeng, D.1    Zhao, J.2    Chung, H.S.3    Guan, Z.4    Raetz, C.R.H.5    Zhou, P.6
  • 53
    • 24044489239 scopus 로고    scopus 로고
    • The global transcriptional response of Escherichia coli to induced sigma 32 protein involves sigma 32 regulon activation followed by inactivation and degradation of sigma 32 in vivo
    • Zhao, K., Liu, M., and Burgess, R.R. (2005) The global transcriptional response of Escherichia coli to induced sigma 32 protein involves sigma 32 regulon activation followed by inactivation and degradation of sigma 32 in vivo. J Biol Chem 280: 17758-17768.
    • (2005) J Biol Chem , vol.280 , pp. 17758-17768
    • Zhao, K.1    Liu, M.2    Burgess, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.