메뉴 건너뛰기




Volumn 32, Issue 17, 2004, Pages 5260-5279

Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: Implications for the origins of chromosome segregation, cell division and viral capsid packaging

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARCHAEAL PROTEIN; BACTERIAL PROTEIN; ENDONUCLEASE; MRE11 PROTEIN; NUCLEASE; PROTEIN FTSK; PROTEIN HERA; RAD50 PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 2; UNCLASSIFIED DRUG; CAPSID PROTEIN; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; FTSK PROTEIN, E COLI; MEMBRANE PROTEIN; VIRUS PROTEIN;

EID: 5144223072     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh828     Document Type: Review
Times cited : (271)

References (108)
  • 3
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FTSZ: Poised at the edge of stability
    • Romberg,L. and Levin,P.A. (2003) Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability. Annu. Rev. Microbiol., 57, 125-154.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 4
    • 0037425628 scopus 로고    scopus 로고
    • Bacterial division: The fellowship of the ring
    • Margolin,W. (2003) Bacterial division: the fellowship of the ring. Curr. Biol., 13, R16-18.
    • (2003) Curr. Biol. , vol.13
    • Margolin, W.1
  • 5
    • 0035196036 scopus 로고    scopus 로고
    • Spatial regulation of cytokinesis in bacteria
    • Margolin,W. (2001) Spatial regulation of cytokinesis in bacteria, Curr. Opin. Microbiol., 4, 647-652.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 647-652
    • Margolin, W.1
  • 6
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • Chen,J.C. and Beckwith,J. (2001) FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol. Microbiol., 42, 395-413.
    • (2001) Mol. Microbiol. , vol.42 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 8
    • 0031786575 scopus 로고    scopus 로고
    • Role of the C terminus of FtsK in Escherichia coli chromosome segregation
    • Yu,X.C.,Weihe,E.K. and Margolin,W. (1998) Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J. Bacteriol., 180, 6424-6428.
    • (1998) J. Bacteriol. , vol.180 , pp. 6424-6428
    • Yu, X.C.1    Weihe, E.K.2    Margolin, W.3
  • 9
    • 0037169328 scopus 로고    scopus 로고
    • FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases
    • Aussel,L., Barre,F.X., Aroyo,M., Stasiak,A., Stasiak,A.Z. and Sherratt,D. (2002) FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell, 108, 195-205.
    • (2002) Cell , vol.108 , pp. 195-205
    • Aussel, L.1    Barre, F.X.2    Aroyo, M.3    Stasiak, A.4    Stasiak, A.Z.5    Sherratt, D.6
  • 12
    • 0036187422 scopus 로고    scopus 로고
    • FtsK: Maxwell's demon?
    • Donachie,W.D. (2002) FtsK: Maxwell's demon? Mol. Cell, 9, 206-207.
    • (2002) Mol. Cell , vol.9 , pp. 206-207
    • Donachie, W.D.1
  • 14
    • 0347504849 scopus 로고    scopus 로고
    • Decatenation of DNA circles by FtsK-dependent Xer site-specific recombination
    • Ip,S.C., Bregu,M., Barre,F.X. and Sherratt,D.J. (2003) Decatenation of DNA circles by FtsK-dependent Xer site-specific recombination. EMBO J., 22, 6399-6407.
    • (2003) EMBO J. , vol.22 , pp. 6399-6407
    • Ip, S.C.1    Bregu, M.2    Barre, F.X.3    Sherratt, D.J.4
  • 15
    • 2442543553 scopus 로고    scopus 로고
    • Asymmetric activation of Xer site-specific recombination by FtsK
    • Massey,T.H., Aussel,L., Barre,F.X. and Sherratt,D.J. (2004) Asymmetric activation of Xer site-specific recombination by FtsK. EMBO Rep., 5, 399-404.
    • (2004) EMBO Rep. , vol.5 , pp. 399-404
    • Massey, T.H.1    Aussel, L.2    Barre, F.X.3    Sherratt, D.J.4
  • 16
    • 0242582268 scopus 로고    scopus 로고
    • A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV
    • Espeli,O., Lee,C. and Marians,K.J. (2003) A physical and functional interaction between Escherichia coli FtsK and topoisomerase IV. J. Biol. Chem., 278, 44639-44644.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44639-44644
    • Espeli, O.1    Lee, C.2    Marians, K.J.3
  • 17
    • 0036568776 scopus 로고    scopus 로고
    • The ESAT-6/WXG100 superfamily - And a new Gram-positive secretion system?
    • Pallen,M.J. (2002) The ESAT-6/WXG100 superfamily - and a new Gram-positive secretion system? Trends Microbiol., 10, 209-212.
    • (2002) Trends Microbiol. , vol.10 , pp. 209-212
    • Pallen, M.J.1
  • 18
    • 2442670846 scopus 로고    scopus 로고
    • A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
    • Constantinesco,F., Forterre,P., Koonin,E.V., Aravind,L. and Elie,C. (2004) A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea. Nucleic Acids Res., 32, 1439-1447.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1439-1447
    • Constantinesco, F.1    Forterre, P.2    Koonin, E.V.3    Aravind, L.4    Elie, C.5
  • 19
    • 0033579554 scopus 로고    scopus 로고
    • Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation
    • Moncalian,G., Cabezon,E., Alkorta,I., Valle,M., Moro,F., Valpuesta,J.M., Goni,F.M. and de La Cruz,F. (1999) Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation. J. Biol. Chem., 274, 36117-36124.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36117-36124
    • Moncalian, G.1    Cabezon, E.2    Alkorta, I.3    Valle, M.4    Moro, F.5    Valpuesta, J.M.6    Goni, F.M.7    de La Cruz, F.8
  • 20
    • 0034053027 scopus 로고    scopus 로고
    • TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58
    • Hamilton,C.M., Lee,H., Li,P.L., Cook,D.M., Piper,K.R., von Bodman,S.B., Lanka,E., Ream,W. and Farrand,S.K. (2000) TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58. J. Bacteriol., 182, 1541-1548.
    • (2000) J. Bacteriol. , vol.182 , pp. 1541-1548
    • Hamilton, C.M.1    Lee, H.2    Li, P.L.3    Cook, D.M.4    Piper, K.R.5    von Bodman, S.B.6    Lanka, E.7    Ream, W.8    Farrand, S.K.9
  • 21
    • 0033037708 scopus 로고    scopus 로고
    • Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter
    • Dang,T.A., Zhou,X.R., Graf,B. and Christie,P.J. (1999) Dimerization of the Agrobacterium tumefaciens VirB4 ATPase and the effect of ATP-binding cassette mutations on the assembly and function of the T-DNA transporter. Mol. Microbiol., 32, 1239-1253.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1239-1253
    • Dang, T.A.1    Zhou, X.R.2    Graf, B.3    Christie, P.J.4
  • 22
    • 0028569497 scopus 로고
    • An essential virulence protein of Agrobacterium tumefaciens, VirB4, requires an intact mononucleotide binding domain to function in transfer of T-DNA
    • Fullner,K.J., Stephens,K.M. and Nester,E.W. (1994) An essential virulence protein of Agrobacterium tumefaciens, VirB4, requires an intact mononucleotide binding domain to function in transfer of T-DNA. Mol. Gen. Genet., 245, 704-715.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 704-715
    • Fullner, K.J.1    Stephens, K.M.2    Nester, E.W.3
  • 23
    • 0027500610 scopus 로고
    • The Agrobacterium tumefaciens virB4 gene product is an essential virulence protein requiring an intact nucleoside triphosphate-binding domain
    • Berger,B.R. and Christie,P.J. (1993) The Agrobacterium tumefaciens virB4 gene product is an essential virulence protein requiring an intact nucleoside triphosphate-binding domain. J. Bacteriol., 175, 1723-1734.
    • (1993) J. Bacteriol. , vol.175 , pp. 1723-1734
    • Berger, B.R.1    Christie, P.J.2
  • 24
    • 0028200971 scopus 로고
    • Promiscuous DNA transfer system of Agrobacterium tumefaciens: Role of the virB operon in sex pilus assembly and synthesis
    • Kado,C.I. (1994) Promiscuous DNA transfer system of Agrobacterium tumefaciens: role of the virB operon in sex pilus assembly and synthesis. Mol. Microbiol., 12, 17-22.
    • (1994) Mol. Microbiol. , vol.12 , pp. 17-22
    • Kado, C.I.1
  • 26
    • 0035252559 scopus 로고    scopus 로고
    • Structural biology. Pumping DNA
    • Egelman,E.H. (2001) Structural biology. Pumping DNA. Nature, 409, 573-575.
    • (2001) Nature , vol.409 , pp. 573-575
    • Egelman, E.H.1
  • 27
    • 0037219192 scopus 로고    scopus 로고
    • A rotary pumping model for helicase function of MCM proteins at a distance from replication forks
    • Laskey,R.A. and Madine,M.A. (2003) A rotary pumping model for helicase function of MCM proteins at a distance from replication forks. EMBO Rep., 4, 26-30.
    • (2003) EMBO Rep. , vol.4 , pp. 26-30
    • Laskey, R.A.1    Madine, M.A.2
  • 29
    • 0036305477 scopus 로고    scopus 로고
    • NurA, a novel 5′-3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea
    • Constantinesco,F., Forterre,P. and Elie,C. (2002) NurA, a novel 5′-3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea. EMBO Rep., 3, 537-542.
    • (2002) EMBO Rep. , vol.3 , pp. 537-542
    • Constantinesco, F.1    Forterre, P.2    Elie, C.3
  • 30
    • 0033828623 scopus 로고    scopus 로고
    • Guilt by association: Contextual information in genome analysis
    • Aravind,L. (2000) Guilt by association: contextual information in genome analysis. Genome Res., 10, 1074-1077,
    • (2000) Genome Res. , vol.10 , pp. 1074-1077
    • Aravind, L.1
  • 31
    • 0034084865 scopus 로고    scopus 로고
    • Who's your neighbor? New computational approaches for functional genomics
    • Galperin,M.Y. and Koonin,E.V. (2000) Who's your neighbor? New computational approaches for functional genomics. Nat. Biotechnol., 18, 609-613.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 609-613
    • Galperin, M.Y.1    Koonin, E.V.2
  • 33
    • 0033940941 scopus 로고    scopus 로고
    • Gene and context: Integrative approaches to genome analysis
    • Huynen,M.J. and Snel,B. (2000) Gene and context: integrative approaches to genome analysis. Adv. Prot. Chem., 54, 345-379.
    • (2000) Adv. Prot. Chem. , vol.54 , pp. 345-379
    • Huynen, M.J.1    Snel, B.2
  • 34
    • 0033823009 scopus 로고    scopus 로고
    • Themes and variations in prokaryotic cell division
    • Margolin,W. (2000) Themes and variations in prokaryotic cell division. FEMS Microbiol. Rev., 24, 531-548.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 531-548
    • Margolin, W.1
  • 36
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame,C., Higgins,D.G. and Heringa,J. (2000) T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol., 302, 205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 37
    • 0037433034 scopus 로고    scopus 로고
    • PCMA: Fast and accurate multiple sequence alignment based on profile consistency
    • Pei,J., Sadreyev,R. and Grishin,N.V. (2003) PCMA: fast and accurate multiple sequence alignment based on profile consistency. Bioinformatics, 19, 427-428.
    • (2003) Bioinformatics , vol.19 , pp. 427-428
    • Pei, J.1    Sadreyev, R.2    Grishin, N.V.3
  • 39
    • 0036132818 scopus 로고    scopus 로고
    • Transmembrane topology prediction methods: A re-assessment and improvement by a consensus method using a dataset of experimentally-characterized transmembrane topologies
    • Ikeda,M., Arai., Lao,D.M. and Shimizu,T. (2002) Transmembrane topology prediction methods: a re-assessment and improvement by a consensus method using a dataset of experimentally-characterized transmembrane topologies. In Silico Biol., 2, 19-33.
    • (2002) Silico Biol. , vol.2 , pp. 19-33
    • Ikeda, M.1    Arai, M.2    Lao, D.M.3    Shimizu, T.4
  • 40
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-model: Internet-based tools for automated comparative protein modelling
    • Peitsch,M.C. (1996) ProMod and Swiss-model: internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans., 24, 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 41
    • 0001339532 scopus 로고
    • A program to produce both detailed and schematic plots of proteins
    • Kraulis,P. (1991) A program to produce both detailed and schematic plots of proteins. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 42
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • Rost,B., Sander,C. and Schneider,R. (1994) PHD - an automatic mail server for protein secondary structure prediction. Comput. Appl. Biosci., 10, 53-60.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 43
    • 0029901637 scopus 로고    scopus 로고
    • Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods
    • Felsenstein,J. (1996) Inferring phylogenies from protein sequences by parsimony, distance, and likelihood methods. Methods Enzymol., 266, 418-427.
    • (1996) Methods Enzymol. , vol.266 , pp. 418-427
    • Felsenstein, J.1
  • 44
    • 0025873443 scopus 로고
    • On the maximum likelihood method in molecular phylogenetics
    • Hasegawa,M., Kishino,H. and Saitou,N. (1991) On the maximum likelihood method in molecular phylogenetics. J. Mol. Evol., 32 443-445.
    • (1991) J. Mol. Evol. , vol.32 , pp. 443-445
    • Hasegawa, M.1    Kishino, H.2    Saitou, N.3
  • 45
    • 0348044549 scopus 로고    scopus 로고
    • Genome trees constructed using five different approaches suggest new major bacterial clades
    • Wolf,Y.I., Rogozin,I.B., Grishin,N.V., Tatusov,R.L. and Koonin,E.V. (2001) Genome trees constructed using five different approaches suggest new major bacterial clades. BMC Evol. Biol., 1, 8.
    • (2001) BMC Evol. Biol. , vol.1 , pp. 8
    • Wolf, Y.I.1    Rogozin, I.B.2    Grishin, N.V.3    Tatusov, R.L.4    Koonin, E.V.5
  • 46
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • Neuwald,A.F., Liu,J.S., Lipman,D.J. and Lawrence,C.E. (1997) Extracting protein alignment models from the sequence database. Nucleic Acids Res., 25, 1665-1677.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1665-1677
    • Neuwald, A.F.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 47
    • 0026784412 scopus 로고
    • The second cholera toxin, Zot, and its plasmid-encoded and phage-encoded homologues constitute a group of putative ATPases with an altered purine NTP-binding motif
    • Koonin,E.V. (1992) The second cholera toxin, Zot, and its plasmid-encoded and phage-encoded homologues constitute a group of putative ATPases with an altered purine NTP-binding motif. FEBS Lett. 312, 3-6.
    • (1992) FEBS Lett. , vol.312 , pp. 3-6
    • Koonin, E.V.1
  • 48
    • 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 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 50
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya,A.E. and Koonin,E.V. (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol., 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 52
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya,M.R., Guo,S., Tabor,S., Richardson,C.C. and Ellenberger,T. (1999) Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell, 99, 167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 53
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton,M.R., Sawaya,M.R., Ellenberger,T. and Wigley,D.B. (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell, 101, 589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 54
    • 0033598667 scopus 로고    scopus 로고
    • Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization
    • Nadanaciva,S., Weber,J., Wilke-Mounts,S. and Senior,A.E. (1999) Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization. Biochemistry, 38, 15493-15499.
    • (1999) Biochemistry , vol.38 , pp. 15493-15499
    • Nadanaciva, S.1    Weber, J.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 55
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe,D.D., Aravind,L., Grishin,N.V. and Koonin,E.V. (2000) The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res., 10, 5-16.
    • (2000) Genome Res. , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 57
    • 0030722725 scopus 로고    scopus 로고
    • G proteins. The arginine finger strikes again
    • Bourne,H.R. (1997) G proteins. The arginine finger strikes again. Nature, 389, 673-674.
    • (1997) Nature , vol.389 , pp. 673-674
    • Bourne, H.R.1
  • 58
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian,M.R., Stege,P., Scheffzek,K. and Wittinghofer,A. (1997) Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nature Struct. Biol. 4, 686-689.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 59
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • Leipe,D.D., Wolf,Y.I., Koonin,E.V. and Aravind,L. (2002) Classification and evolution of P-loop GTPases and related ATPases. J. Mol. Biol., 317, 41-72.
    • (2002) J. Mol. Biol. , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 60
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe,D.D., Koonin,E.V. and Aravind,L. (2003) Evolution and classification of P-loop kinases and related proteins. J. Mol. Biol. 333, 781-815.
    • (2003) J. Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 62
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm,L. and Sander,C. (1995) Dali: a network tool for protein structure comparison. Trends Biochem. Sci., 20, 478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 63
    • 0037106323 scopus 로고    scopus 로고
    • Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases
    • Mitchell,M.S., Matsuzaki,S., Imai,S. and Rao,V.B. (2002) Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Res., 30, 4009-4021.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4009-4021
    • Mitchell, M.S.1    Matsuzaki, S.2    Imai, S.3    Rao, V.B.4
  • 64
    • 0033523085 scopus 로고    scopus 로고
    • Structure/function of the beta-barrel domain of F1-ATPase in the yeast Saccharomyces cerevisiae
    • Bakhtiari,N., Lai-Zhang,J., Yao,B. and Mueller,D.M. (1999) Structure/function of the beta-barrel domain of F1-ATPase in the yeast Saccharomyces cerevisiae. J. Biol. Chem., 274, 16363-16369.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16363-16369
    • Bakhtiari, N.1    Lai-Zhang, J.2    Yao, B.3    Mueller, D.M.4
  • 66
    • 0242384036 scopus 로고    scopus 로고
    • The outs and ins of bacterial type IV secretion substrates
    • Ding,Z., Atmakuri,K. and Christie,P.J. (2003) The outs and ins of bacterial type IV secretion substrates. Trends Microbiol., 11, 527-535.
    • (2003) Trends Microbiol. , vol.11 , pp. 527-535
    • Ding, Z.1    Atmakuri, K.2    Christie, P.J.3
  • 69
    • 0035374570 scopus 로고    scopus 로고
    • Zonula occludens toxin structure-function analysis. Identification of the fragment biologically active on tight junctions and of the zonulin receptor binding domain
    • Di Pierro,M., Lu,R., Uzzau,S., Wang,W., Margaretten,K., Pazzani,C., Maimone,F. and Fasano,A. (2001) Zonula occludens toxin structure-function analysis. Identification of the fragment biologically active on tight junctions and of the zonulin receptor binding domain. J. Biol. Chem., 276, 19160-19165.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19160-19165
    • Di Pierro, M.1    Lu, R.2    Uzzau, S.3    Wang, W.4    Margaretten, K.5    Pazzani, C.6    Maimone, F.7    Fasano, A.8
  • 70
    • 0027413261 scopus 로고
    • Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases
    • Koonin,E.V., Senkevich,T.G. and Chernos,V.I. (1993) Gene A32 product of vaccinia virus may be an ATPase involved in viral DNA packaging as indicated by sequence comparisons with other putative viral ATPases. Virus Genes, 7, 89-94.
    • (1993) Virus Genes , vol.7 , pp. 89-94
    • Koonin, E.V.1    Senkevich, T.G.2    Chernos, V.I.3
  • 71
    • 0035167322 scopus 로고    scopus 로고
    • Common origin of four diverse families of large eukaryotic DNA viruses
    • Iyer,L.M., Aravind,L. and Koonin,E.V. (2001) Common origin of four diverse families of large eukaryotic DNA viruses. J. Virol., 75, 11720-11734.
    • (2001) J. Virol. , vol.75 , pp. 11720-11734
    • Iyer, L.M.1    Aravind, L.2    Koonin, E.V.3
  • 73
    • 0036606136 scopus 로고    scopus 로고
    • A novel family of mobile genetic elements is limited to the germline genome in Tetrahymena thermophila
    • Wuitschick,J.D., Gershan,J.A., Lochowicz,A.J., Li,S. and Karrer,K.M. (2002) A novel family of mobile genetic elements is limited to the germline genome in Tetrahymena thermophila. Nucleic Acids Res. 30, 2524-2537.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2524-2537
    • Wuitschick, J.D.1    Gershan, J.A.2    Lochowicz, A.J.3    Li, S.4    Karrer, K.M.5
  • 75
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication proteins
    • Edgell,D.R. and Doolittle,W.F. (1997) Archaea and the origin(s) of DNA replication proteins. Cell, 89, 995-998.
    • (1997) Cell , vol.89 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 76
    • 0033199713 scopus 로고    scopus 로고
    • Did DNA replication evolve twice independently?
    • Leipe,D.D., Aravind,L. and Koonin,E.V. (1999) Did DNA replication evolve twice independently? Nucleic Acids Res., 27 3389-3401.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3389-3401
    • Leipe, D.D.1    Aravind, L.2    Koonin, E.V.3
  • 78
    • 1642540251 scopus 로고    scopus 로고
    • Cell division: Burning the spindle at both ends
    • Heald,R.W. (2004) Cell division: burning the spindle at both ends. Nature, 427, 300-301.
    • (2004) Nature , vol.427 , pp. 300-301
    • Heald, R.W.1
  • 80
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind,L., Galperin,M.Y. and Koonin,E.V. (1998) The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci., 23, 127-129.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 81
    • 0042732955 scopus 로고    scopus 로고
    • The role of yeast DNA 3′-phosphatase Tpp1 and rad1/Rad10 endonuclease in processing spontaneous and induced base lesions
    • Karumbati,A.S., Deshpande,R.A., Jilani,A., Vance,J.R., Ramotar,D. and Wilson,T.E. (2003) The role of yeast DNA 3′ -phosphatase Tpp1 and rad1/Rad10 endonuclease in processing spontaneous and induced base lesions. J. Biol. Chem., 278, 31434-31443.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31434-31443
    • Karumbati, A.S.1    Deshpande, R.A.2    Jilani, A.3    Vance, J.R.4    Ramotar, D.5    Wilson, T.E.6
  • 82
    • 0033167929 scopus 로고    scopus 로고
    • Structural maintenance of chromosomes (SMC) proteins: Conserved molecular properties for multiple biological functions
    • Strunnikov,A.V. and Jessberger,R. (1999) Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions. Eur. J. Biochem., 263, 6-13.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 6-13
    • Strunnikov, A.V.1    Jessberger, R.2
  • 83
    • 0036792404 scopus 로고    scopus 로고
    • The many functions of SMC proteins in chromosome dynamics
    • Jessberger,R. (2002) The many functions of SMC proteins in chromosome dynamics. Nature Rev. Mol. Cell Biol., 3, 767-778.
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 767-778
    • Jessberger, R.1
  • 84
    • 0142186242 scopus 로고    scopus 로고
    • The MRN complex: Coordinating and mediating the response to broken chromosomes
    • van den Bosch,M., Bree,R.T. and Lowndes,N.F. (2003) The MRN complex: coordinating and mediating the response to broken chromosomes. EMBO Rep., 4, 844-849.
    • (2003) EMBO Rep. , vol.4 , pp. 844-849
    • van den Bosch, M.1    Bree, R.T.2    Lowndes, N.F.3
  • 85
    • 1242294388 scopus 로고    scopus 로고
    • Association of Mre11p with double-strand break sites during yeast meiosis
    • Borde,V., Lin,W., Novikov,E., Petrini,J.H., Lichten,M. and Nicolas,A. (2004) Association of Mre11p with double-strand break sites during yeast meiosis. Mol. Cell, 13, 389-401.
    • (2004) Mol. Cell , vol.13 , pp. 389-401
    • Borde, V.1    Lin, W.2    Novikov, E.3    Petrini, J.H.4    Lichten, M.5    Nicolas, A.6
  • 87
    • 0035035578 scopus 로고    scopus 로고
    • Type IV secretion: Intercellular transfer of macromolecules by systems ancestrally related to conjugation machines
    • Christie,P.J. (2001) Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines. Mol. Microbiol., 40, 294-305.
    • (2001) Mol. Microbiol. , vol.40 , pp. 294-305
    • Christie, P.J.1
  • 88
    • 0029007928 scopus 로고
    • DNA processing reactions in bacterial conjugation
    • Lanka,E. and Wilkins,B.M. (1995) DNA processing reactions in bacterial conjugation. Annu. Rev. Biochem., 64, 141-169.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 141-169
    • Lanka, E.1    Wilkins, B.M.2
  • 89
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
    • Ilyina,T.V. and Koonin,E.V. (1992) Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria. Nucleic Acids Res., 20, 3279-3285.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 90
    • 0242542025 scopus 로고    scopus 로고
    • Structural insights into single-stranded DNA binding and cleavage by F factor TraI
    • Datta,S., Larkin,C. and Schildbach,J.F. (2003) Structural insights into single-stranded DNA binding and cleavage by F factor TraI. Structure (Camb.), 11, 1369-1379.
    • (2003) Structure (Camb.) , vol.11 , pp. 1369-1379
    • Datta, S.1    Larkin, C.2    Schildbach, J.F.3
  • 92
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • Anantharaman,V. and Aravind,L. (2003) Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol., 4, R11.
    • (2003) Genome Biol. , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 93
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • Moazed,D. (2001) Enzymatic activities of Sir2 and chromatin silencing. Curr. Opin. Cell Biol., 13, 232-238.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 232-238
    • Moazed, D.1
  • 94
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min,J., Landry,J., Sternglanz,R. and Xu,R.M. (2001) Crystal structure of a SIR2 homolog-NAD complex. Cell, 105, 269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 95
    • 1542298916 scopus 로고    scopus 로고
    • Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
    • Zhao,K., Chai,X. and Marmorstein,R. (2004) Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. J. Mol. Biol., 337, 731-741.
    • (2004) J. Mol. Biol. , vol.337 , pp. 731-741
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 96
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide
    • Zhao,K., Chai,X. and Marmorstein,R. (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide. Structure (Camb.), 11, 1403-1411.
    • (2003) Structure (Camb.) , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 99
    • 0036920683 scopus 로고    scopus 로고
    • Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily
    • Mazumder,R., Iyer,L.M., Vasudevan,S. and Aravind,L. (2002) Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily. Nucleic Acids Res., 30, 5229-5243.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5229-5243
    • Mazumder, R.1    Iyer, L.M.2    Vasudevan, S.3    Aravind, L.4
  • 100
    • 0030200347 scopus 로고    scopus 로고
    • A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins
    • Koonin,E.V. (1996) A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins. Trends Biochem. Sci., 21, 242-243.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 242-243
    • Koonin, E.V.1
  • 101
    • 0345869711 scopus 로고    scopus 로고
    • Generation of the BfiI restriction endonuclease from the fusion of a DNA recognition domain to a non-specific nuclease from the phospholipase D superfamily
    • Zaremba,M., Urbanke,C., Halford,S.E. and Siksnys,V. (2004) Generation of the BfiI restriction endonuclease from the fusion of a DNA recognition domain to a non-specific nuclease from the phospholipase D superfamily. J. Mol. Biol., 336, 81-92.
    • (2004) J. Mol. Biol. , vol.336 , pp. 81-92
    • Zaremba, M.1    Urbanke, C.2    Halford, S.E.3    Siksnys, V.4
  • 102
    • 0033569666 scopus 로고    scopus 로고
    • Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes
    • Pouliot,J.J., Yao,K.C., Robertson,C.A. and Nash,H.A. (1999) Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes. Science, 286, 552-555.
    • (1999) Science , vol.286 , pp. 552-555
    • Pouliot, J.J.1    Yao, K.C.2    Robertson, C.A.3    Nash, H.A.4
  • 103
    • 0036046771 scopus 로고    scopus 로고
    • Evolution of gene fusions: Horizontal transfer versus independent events
    • Yanai,I., Wolf,Y.I. and Koonin,E.V. (2002) Evolution of gene fusions: horizontal transfer versus independent events. Genome Biol. 3, research0024.
    • (2002) Genome Biol. , vol.3
    • Yanai, I.1    Wolf, Y.I.2    Koonin, E.V.3
  • 104
    • 0030714064 scopus 로고    scopus 로고
    • Repair by recombination of DNA containing a palindromic sequence
    • Leach,D.R., Okely,E.A. and Pinder,D.J. (1997) Repair by recombination of DNA containing a palindromic sequence. Mol. Microbiol., 26, 597-606.
    • (1997) Mol. Microbiol. , vol.26 , pp. 597-606
    • Leach, D.R.1    Okely, E.A.2    Pinder, D.J.3
  • 105
    • 0034663517 scopus 로고    scopus 로고
    • The roles of mutS, sbcCD and recA in the propagation of TGG repeats in Escherichia coli
    • Pan,X. and Leach,D.R. (2000) The roles of mutS, sbcCD and recA in the propagation of TGG repeats in Escherichia coli. Nucleic Acids Res., 28, 3178-3184.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3178-3184
    • Pan, X.1    Leach, D.R.2
  • 107
    • 1642344759 scopus 로고    scopus 로고
    • Structural/functional homology between the bacterial and eukaryotic cytoskeletons
    • Amos,L.A., van den Ent,F. and Lowe,J. (2004) Structural/functional homology between the bacterial and eukaryotic cytoskeletons. Curr. Opin. Cell Biol., 16, 24-31.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 24-31
    • Amos, L.A.1    van den Ent, F.2    Lowe, J.3
  • 108
    • 4043121007 scopus 로고    scopus 로고
    • The SHS2 module is a common structural theme in functionally diverse protein groups, like Rpb7p, FtsA, GyrI, and MTH1598/TM1083 superfamilies
    • in press
    • Anantharaman,V. and Aravind,L. (2004) The SHS2 module is a common structural theme in functionally diverse protein groups, like Rpb7p, FtsA, GyrI, and MTH1598/TM1083 superfamilies. Proteins, in press.
    • (2004) Proteins
    • Anantharaman, V.1    Aravind, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.