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Volumn 230, Issue 2, 2004, Pages 241-249

The yjoB gene of Bacillus subtilis encodes a protein that is a novel member of the AAA family

Author keywords

AAA family; ATPase; Citrate synthase; ftsH; yjoB

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID; BACTERIAL PROTEIN; CITRATE SYNTHASE;

EID: 1642481289     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00912-1     Document Type: Article
Times cited : (5)

References (43)
  • 1
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri F., Duguet M. A 200-amino acid ATPase module in search of a basic function. BioEssays. 17:1995;639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 2
    • 1642443761 scopus 로고
    • The AAA-team: Related ATPases making it and breaking it in the cell
    • Patel S., Latterich M. The AAA-team: Related ATPases making it and breaking it in the cell. Trends Cell Biol. 8:1995;65-71.
    • (1995) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 3
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure-diverse function
    • + superfamily ATPases: common structure-diverse function. Genes Cells. 6:2001;575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 4
    • 0030018173 scopus 로고    scopus 로고
    • Substitution of fifty four homologue (Ffh) in Escherichia coli with the mammalian 54-kDa protein of signal-recognition particle
    • Patel S., Austen B.M. Substitution of fifty four homologue (Ffh) in Escherichia coli with the mammalian 54-kDa protein of signal-recognition particle. Eur. J. Biochem. 238:1996;760-768.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 760-768
    • Patel, S.1    Austen, B.M.2
  • 5
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 6
    • 0025965277 scopus 로고
    • PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases
    • Erdmann R., Wieber F.F., Flessau A., Rytka J., Beyer A., Fröhlich K., Kunau W. PAS1, a yeast gene required for peroxisome biogenesis, encodes a member of a novel family of putative ATPases. Cell. 64:1991;499-510.
    • (1991) Cell , vol.64 , pp. 499-510
    • Erdmann, R.1    Wieber, F.F.2    Flessau, A.3    Rytka, J.4    Beyer, A.5    Fröhlich, K.6    Kunau, W.7
  • 7
    • 0032965905 scopus 로고    scopus 로고
    • FtsH - A single-chain charonin?
    • Schumann W. FtsH - a single-chain charonin? FEMS Microbiol. Rev. 23:1999;1-11.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 1-11
    • Schumann, W.1
  • 9
    • 0036773132 scopus 로고    scopus 로고
    • Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8
    • Niwa H., Tsuchiya D., Makyio H., Yoshida M., Morikawa K. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8. Structure. 10:2002;1415-1423.
    • (2002) Structure , vol.10 , pp. 1415-1423
    • Niwa, H.1    Tsuchiya, D.2    Makyio, H.3    Yoshida, M.4    Morikawa, K.5
  • 10
    • 0036054289 scopus 로고    scopus 로고
    • The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Å resolution
    • Krzywda S., Brzozowski A.M., Verma C., Karata K., Ogura T., Wilkinson A.J. The crystal structure of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli at 1.5 Å resolution. Structure. 10:2002;1073-1083.
    • (2002) Structure , vol.10 , pp. 1073-1083
    • Krzywda, S.1    Brzozowski, A.M.2    Verma, C.3    Karata, K.4    Ogura, T.5    Wilkinson, A.J.6
  • 11
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes
    • Zwickl P., Ng D., Woo K.M., Klenk H.P., Goldberg A.L. An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes. J. Biol. Chem. 274:1999;26008-26014.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26008-26014
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.P.4    Goldberg, A.L.5
  • 12
    • 0035716877 scopus 로고    scopus 로고
    • The proteasome: A supramolecular assembly designed for controlled proteolysis
    • Zwickl P., Seemüller E., Kapelari B., Baumeister W. The proteasome: a supramolecular assembly designed for controlled proteolysis. Adv. Protein Chem. 59:2001;187-222.
    • (2001) Adv. Protein Chem. , vol.59 , pp. 187-222
    • Zwickl, P.1    Seemüller, E.2    Kapelari, B.3    Baumeister, W.4
  • 14
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst F., Ogasawara N., Moszer I., et al. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature. 390:1997;249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 15
    • 0031803530 scopus 로고    scopus 로고
    • Polypeptide binding of Escherichia coli FtsH (HflB)
    • Akiyama Y., Ehrmann M., Kihara A., Ito K. Polypeptide binding of Escherichia coli FtsH (HflB). Mol. Microbiol. 28:1998;803-812.
    • (1998) Mol. Microbiol. , vol.28 , pp. 803-812
    • Akiyama, Y.1    Ehrmann, M.2    Kihara, A.3    Ito, K.4
  • 16
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • Leonhard K., Stiegler A., Neupert W., Langer T. Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature. 398:1999;348-351.
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 20
    • 0001615272 scopus 로고
    • Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate
    • Spizizen J. Transformation of biochemically deficient strains of Bacillus subtilis by deoxyribonucleate. Proc. Natl. Acad. Sci. USA. 44:1958;407-408.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 407-408
    • Spizizen, J.1
  • 21
    • 0014945433 scopus 로고
    • Calcium dependent bacteriophage DNA infection
    • Mandel M., Higa A. Calcium dependent bacteriophage DNA infection. J. Mol. Biol. 53:1970;154-162.
    • (1970) J. Mol. Biol. , vol.53 , pp. 154-162
    • Mandel, M.1    Higa, A.2
  • 22
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos C., Spizizen J. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:1961;741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 23
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner V., Dervyn E., Ehrlich S.D. A vector for systematic gene inactivation in Bacillus subtilis. Microbiology. 144:1998;3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 25
    • 0030571520 scopus 로고    scopus 로고
    • Integrative vectors for constructing single-copy transcriptional fusions between Bacillus subtilis promoters and various reporter genes encoding heat-stable enzymes
    • Mogk A., Hayward R., Schumann W. Integrative vectors for constructing single-copy transcriptional fusions between Bacillus subtilis promoters and various reporter genes encoding heat-stable enzymes. Gene. 182:1996;33-36.
    • (1996) Gene , vol.182 , pp. 33-36
    • Mogk, A.1    Hayward, R.2    Schumann, W.3
  • 26
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues
    • Hochuli E., Döbeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues. J. Chromatogr. 411:1987;177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Döbeli, H.2    Schacher, A.3
  • 27
    • 0029949534 scopus 로고    scopus 로고
    • The genes lepA and hemN form a bicistronic operon in Bacillus subtilis
    • Homuth G., Heinemann M., Zuber U., Schumann W. The genes lepA and hemN form a bicistronic operon in Bacillus subtilis. Microbiology. 142:1996;1641-1649.
    • (1996) Microbiology , vol.142 , pp. 1641-1649
    • Homuth, G.1    Heinemann, M.2    Zuber, U.3    Schumann, W.4
  • 28
    • 0031030242 scopus 로고    scopus 로고
    • Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis
    • Turgay K., Hamoen L.W., Venema G., Dubnau D. Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis. Genes Dev. 11:1997;119-128.
    • (1997) Genes Dev. , vol.11 , pp. 119-128
    • Turgay, K.1    Hamoen, L.W.2    Venema, G.3    Dubnau, D.4
  • 29
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill R., Dowhan W., Wickner W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell. 60:1990;271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 30
  • 31
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner J., Grallert H., Jakob U. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol. 290:1998;323-338.
    • (1998) Methods Enzymol. , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 32
    • 0035861999 scopus 로고    scopus 로고
    • Dynamic association of trigger factor with protein substrates
    • Maier R., Scholz C., Schmid F.X. Dynamic association of trigger factor with protein substrates. J. Mol. Biol. 14:2001;1181-1190.
    • (2001) J. Mol. Biol. , vol.14 , pp. 1181-1190
    • Maier, R.1    Scholz, C.2    Schmid, F.X.3
  • 33
    • 0031029046 scopus 로고    scopus 로고
    • Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
    • Scholz C., Stoller G., Zarnt T., Fischer G., Schmid F.X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16:1997;54-58.
    • (1997) EMBO J. , vol.16 , pp. 54-58
    • Scholz, C.1    Stoller, G.2    Zarnt, T.3    Fischer, G.4    Schmid, F.X.5
  • 34
    • 0027212676 scopus 로고
    • Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase
    • Popham D.L., Setlow P. Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase. J. Bacteriol. 175:1993;2917-2925.
    • (1993) J. Bacteriol. , vol.175 , pp. 2917-2925
    • Popham, D.L.1    Setlow, P.2
  • 35
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:1999;27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Souge, J.L.3    Koonin, E.V.4
  • 36
    • 0026013244 scopus 로고
    • Molecular chaperones and protein translocation across the Escherichia coli inner membrane
    • Kumamoto C.A. Molecular chaperones and protein translocation across the Escherichia coli inner membrane. Mol. Microbiol. 5:1991;19-22.
    • (1991) Mol. Microbiol. , vol.5 , pp. 19-22
    • Kumamoto, C.A.1
  • 37
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren S.J., Normark S., Abraham S.N. Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu. Rev. Microbiol. 45:1991;383-415.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3
  • 38
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1999;1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 40
    • 0018289188 scopus 로고
    • Mapping of genes determining nonpermissiveness and host-specific restriction to bacteriophages in Bacillus subtilis Marburg
    • Saito H., Shibata T., Ando T. Mapping of genes determining nonpermissiveness and host-specific restriction to bacteriophages in Bacillus subtilis Marburg. Mol. Gen. Genet. 170:1979;117-122.
    • (1979) Mol. Gen. Genet. , vol.170 , pp. 117-122
    • Saito, H.1    Shibata, T.2    Ando, T.3
  • 41
    • 0030849142 scopus 로고    scopus 로고
    • The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
    • Mogk A., Homuth G., Scholz C., Kim L., Schmid F.X., Schumann W. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J. 16:1997;4579-4590.
    • (1997) EMBO J. , vol.16 , pp. 4579-4590
    • Mogk, A.1    Homuth, G.2    Scholz, C.3    Kim, L.4    Schmid, F.X.5    Schumann, W.6
  • 42
    • 0034047383 scopus 로고    scopus 로고
    • The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation
    • Wehrl W., Niederweis M., Schumann W. The FtsH protein accumulates at the septum of Bacillus subtilis during cell division and sporulation. J. Bacteriol. 182:2000;3870-3873.
    • (2000) J. Bacteriol. , vol.182 , pp. 3870-3873
    • Wehrl, W.1    Niederweis, M.2    Schumann, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.