메뉴 건너뛰기




Volumn 86, Issue 7, 2004, Pages 431-438

Effects of two cis-acting mutations on the regulation and expression of release factor one in Escherichia coli

Author keywords

Growth rate control; hemA; Promoters; RF1; Translation initiation

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL RNA; CIS ACTING ELEMENT; RELEASE FACTOR 1; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 4143057005     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2004.06.009     Document Type: Article
Times cited : (5)

References (30)
  • 1
    • 0034326431 scopus 로고    scopus 로고
    • Translational termination comes of age
    • Kisselev L.L., and Buckingham R.H. Translational termination comes of age TIBS 25 2000 561 566
    • (2000) TIBS , vol.25 , pp. 561-566
    • Kisselevbuckingham, R.H.L.L.1    And2
  • 2
    • 0024060925 scopus 로고
    • Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli
    • Kawakami K., Jönsson Y.H., Björk G.R., Ikeda H., and Nakamura Y. Chromosomal location and structure of the operon encoding peptide-chain-release factor 2 of Escherichia coli Proc. Natl. Acad. Sci. USA 85 1988 5620 5624
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5620-5624
    • Kawakami, K.1    Jönsson, Y.H.2    Björk, G.R.3    Ikedanakamura, Y.H.4    And5
  • 3
    • 0022547355 scopus 로고
    • Expression of peptide release factor 2 requires high-efficiency frameshift
    • Craigen W.J., and Caskey C.T. Expression of peptide release factor 2 requires high-efficiency frameshift Nature 322 1986 273 275
    • (1986) Nature , vol.322 , pp. 273-275
    • Craigencaskey, C.T.W.J.1    And2
  • 4
    • 0022896751 scopus 로고
    • Mapping and complementation studies of the gene for release factor 1
    • Rydén M., Murphy J., Martin R., Isaksson L., and Gallant J. Mapping and complementation studies of the gene for release factor 1 J. Bacteriol. 168 1986 1066 1069
    • (1986) J. Bacteriol. , vol.168 , pp. 1066-1069
    • Rydén, M.1    Murphy, J.2    Martin, R.3    Isakssongallant, J.L.4    And5
  • 5
    • 0001918155 scopus 로고    scopus 로고
    • Biosynthesis of hemes
    • second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. American Society for Microbiology Washington, DC
    • Beale S.I. Biosynthesis of hemes second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. Escherichia coli and Salmonella: Cellular and Molecular Biology 1996 American Society for Microbiology Washington, DC 731 748
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 731-748
    • Beale, S.I.1
  • 6
    • 0030746342 scopus 로고    scopus 로고
    • Role of the hemA gene product and δ-aminolevulinic acid in regulation of Escherichia coli heme synthesis
    • Verderber E., Lucast L.J., van Dehy J.A., Cozart P., Etter J.B., and Best E.A. Role of the hemA gene product and δ-aminolevulinic acid in regulation of Escherichia coli heme synthesis J. Bacteriol. 179 1997 4583 4590
    • (1997) J. Bacteriol. , vol.179 , pp. 4583-4590
    • Verderber, E.1    Lucast, L.J.2    Van Dehy, J.A.3    Cozart, P.4    Etterbest, E.A.J.B.5    And6
  • 7
    • 0028797882 scopus 로고
    • Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli
    • Nakayashiki T., Nishimura K., and Inokuchi H. Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli Gene 153 1995 67 70
    • (1995) Gene , vol.153 , pp. 67-70
    • Nakayashiki, T.1    Nishimurainokuchi, H.K.2    And3
  • 9
    • 0037022398 scopus 로고    scopus 로고
    • HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination
    • Nakahigashi K., Kubo N., Narita S.-I., Shimaoka T., Goto S., Oshima T., Mori H., Maeda M., Wada C., and Inokuchi H. HemK, a class of protein methyl transferase with similarity to DNA methyl transferases, methylates polypeptide chain release factors, and hemK knockout induces defects in translational termination Proc. Natl. Acad. Sci. USA 99 2002 1473 1478
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1473-1478
    • Nakahigashi, K.1    Kubo, N.2    Narita, S.-I.3    Shimaoka, T.4    Goto, S.5    Oshima, T.6    Mori, H.7    Maeda, M.8    Wadainokuchi, H.C.9    And10
  • 10
    • 0032962415 scopus 로고    scopus 로고
    • A HilA-independent pathway to Salmonella typhimurium invasion gene transcription
    • Rakeman J.L., Bonifield H.R., and Miller S.I. A HilA-independent pathway to Salmonella typhimurium invasion gene transcription J. Bacteriol. 181 1999 3096 3104
    • (1999) J. Bacteriol. , vol.181 , pp. 3096-3104
    • Rakeman, J.L.1    Bonifieldmiller, S.I.H.R.2    And3
  • 11
    • 0029084375 scopus 로고
    • Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12
    • Strohmaier H., Remler P., Renner W., and Högenauer G. Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12 J. Bacteriol. 177 1995 4488 4500
    • (1995) J. Bacteriol. , vol.177 , pp. 4488-4500
    • Strohmaier, H.1    Remler, P.2    Renner, W.3    Högenauer, G.4
  • 12
    • 0024724030 scopus 로고
    • Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene
    • Verkamp E., and Chelm B.K. Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene J. Bacteriol. 171 1989 4728 4735
    • (1989) J. Bacteriol. , vol.171 , pp. 4728-4735
    • Verkampchelm, B.K.E.1    And2
  • 13
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama S.-I., Yokota N., and Tokuda H. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli EMBO J. 16 1997 6947 6955
    • (1997) EMBO J. , vol.16 , pp. 6947-6955
    • Matsuyama, S.-I.1    Yokotatokuda, H.N.2    And3
  • 14
    • 0344361618 scopus 로고    scopus 로고
    • Regulation of heme biosynthesis in Salmonella typhimurium: Activity of glutamyl-tRNA reductase (hema) is greatly elevated during heme limitation by a mechanism, which increases abundance of the protein
    • Wang L.Y., Brown L., Elliott M., and Elliott T. Regulation of heme biosynthesis in Salmonella typhimurium: activity of glutamyl-tRNA reductase (hema) is greatly elevated during heme limitation by a mechanism, which increases abundance of the protein J. Bacteriol. 179 1997 2907 2914
    • (1997) J. Bacteriol. , vol.179 , pp. 2907-2914
    • Wang, L.Y.1    Brown, L.2    Elliottelliott, T.M.3    And4
  • 15
    • 0032986721 scopus 로고    scopus 로고
    • Conditional stability of HemA protein (Glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium
    • Wang L., Elliott M., and Elliott T. Conditional stability of HemA protein (Glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium J. Bacteriol. 181 1999 1211 1219
    • (1999) J. Bacteriol. , vol.181 , pp. 1211-1219
    • Wang, L.1    Elliottelliott, T.M.2    And3
  • 16
    • 0028357882 scopus 로고
    • The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli
    • Adamski F.M., McCaughan K.K., Jørgensen F., Kurland C.G., and Tate W.P. The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli J. Mol. Biol. 238 1994 302 308
    • (1994) J. Mol. Biol. , vol.238 , pp. 302-308
    • Adamski, F.M.1    McCaughan, K.K.2    Jørgensen, F.3    Kurlandtate, W.P.C.G.4    And5
  • 17
    • 0021939774 scopus 로고
    • Isolation and characterization of antisuppressor mutations in Escherichia coli
    • Sullivan M.A., and Bock R.M. Isolation and characterization of antisuppressor mutations in Escherichia coli J. Bacteriol. 161 1985 377 384
    • (1985) J. Bacteriol. , vol.161 , pp. 377-384
    • Sullivanbock, R.M.M.A.1    And2
  • 19
    • 0017357987 scopus 로고    scopus 로고
    • Chemical measurements of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli
    • Neidhardt F.C., Bloch P.L., Pedersen S., and Reeh S. Chemical measurements of steady-state levels of ten aminoacyl-transfer ribonucleic acid synthetases in Escherichia coli J. Bacteriol. 129 1997 378 387
    • (1997) J. Bacteriol. , vol.129 , pp. 378-387
    • Neidhardt, F.C.1    Bloch, P.L.2    Pedersenreeh, S.S.3    And4
  • 20
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons R.W., Houman F., and Kleckner N. Improved single and multicopy lac-based cloning vectors for protein and operon fusions Gene 53 1987 85 96
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houmankleckner, N.F.2    And3
  • 23
    • 0027483417 scopus 로고
    • Ribosome activity and modification of 16S rRNA are influenced by deletion of ribosomal protein S20
    • Rydén-Aulin M., Zhang S., Kylsten P., and Isaksson L.A. Ribosome activity and modification of 16S rRNA are influenced by deletion of ribosomal protein S20 Mol. Microbiol. 7 1993 983 992
    • (1993) Mol. Microbiol. , vol.7 , pp. 983-992
    • Rydén-Aulin, M.1    Zhang, S.2    Kylsten, P.3    Isaksson, L.A.4
  • 25
    • 0003174053 scopus 로고    scopus 로고
    • The stringent response
    • second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B.N. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. American Society for Microbiology Washington, DC
    • Cashel M., Gentry D.R., Hernandez V.J., and Vinella D. The stringent response second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B.N. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. Escherichia coli and Salmonella: Cellular and Molecular Biology 1996 American Society for Microbiology Washington, DC 1458 1496
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1458-1496
    • Cashel, M.1    Gentry, D.R.2    Hernandezvinella, D.V.J.3    And4
  • 26
    • 0347517767 scopus 로고    scopus 로고
    • Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli
    • Mora L., Zavialov A.V., Ehrenberg M., and Buckingham R.H. Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli Mol. Microbiol. 50 2003 1467 1476
    • (2003) Mol. Microbiol. , vol.50 , pp. 1467-1476
    • Mora, L.1    Zavialov, A.V.2    Ehrenbergbuckingham, R.H.M.3    And4
  • 27
    • 0035951305 scopus 로고    scopus 로고
    • Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro
    • Barker M.M., Gaal T., Josaitis C.A., and Gourse R.L. Mechanism of regulation of transcription initiation by ppGpp. I. Effects of ppGpp on transcription initiation in vivo and in vitro J. Mol. Biol. 305 2001 673 688
    • (2001) J. Mol. Biol. , vol.305 , pp. 673-688
    • Barker, M.M.1    Gaal, T.2    Josaitisgourse, R.L.C.A.3    And4
  • 28
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids J. Mol. Biol. 166 1983 557 580
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 29
    • 0002739483 scopus 로고    scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B.N. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. American Society for Microbiology Washington, DC
    • Bachmann B.J. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12 second ed Neidhardt F.C. Curtiss R. III Ingraham J.L. Lin E.C.C. Low K.B.N. Magasanik B. Reznikoff W.S. Riley M. Schaechter M. Umbarger H.E. Escherichia coli and Salmonella: Cellular and Molecular Biology 1996 American Society for Microbiology Washington, DC 2460 2488
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 2460-2488
    • Bachmann, B.J.1
  • 30
    • 0027251266 scopus 로고
    • The Escherichia coli K-12 "wild Types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels
    • Jensen K.F. The Escherichia coli K-12 "Wild Types" W3110 and MG1655 have an rph frameshift mutation that leads to pyrimidine starvation due to low pyrE expression levels J. Bacteriol. 175 1993 3401 3407
    • (1993) J. Bacteriol. , vol.175 , pp. 3401-3407
    • Jensen, K.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.