메뉴 건너뛰기




Volumn 14, Issue 4, 2016, Pages 679-685

Operon Gene Order Is Optimized for Ordered Protein Complex Assembly

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; BACTERIAL PROTEIN; PROTEIN BINDING;

EID: 84958123338     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.12.085     Document Type: Article
Times cited : (82)

References (32)
  • 2
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: a fingerprint of proteins that physically interact
    • Dandekar T., Snel B., Huynen M., Bork P. Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem. Sci. 1998, 23:324-328.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 3
    • 84855261941 scopus 로고    scopus 로고
    • Widespread cotranslational formation of protein complexes
    • Duncan C.D.S., Mata J. Widespread cotranslational formation of protein complexes. PLoS Genet. 2011, 7:e1002398.
    • (2011) PLoS Genet. , vol.7 , pp. e1002398
    • Duncan, C.D.S.1    Mata, J.2
  • 6
    • 7644223774 scopus 로고    scopus 로고
    • Why is transcription coupled to translation in bacteria?
    • Gowrishankar J., Harinarayanan R. Why is transcription coupled to translation in bacteria?. Mol. Microbiol. 2004, 54:598-603.
    • (2004) Mol. Microbiol. , vol.54 , pp. 598-603
    • Gowrishankar, J.1    Harinarayanan, R.2
  • 7
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernández H., Robinson C.V. Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat. Protoc. 2007, 2:715-726.
    • (2007) Nat. Protoc. , vol.2 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 9
    • 52649130704 scopus 로고    scopus 로고
    • Protein-protein interaction and quaternary structure
    • Janin J., Bahadur R.P., Chakrabarti P. Protein-protein interaction and quaternary structure. Q. Rev. Biophys. 2008, 41:133-180.
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 133-180
    • Janin, J.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 11
    • 66249146869 scopus 로고    scopus 로고
    • Stochasticity in protein levels drives colinearity of gene order in metabolic operons of Escherichia coli
    • Kovács K., Hurst L.D., Papp B. Stochasticity in protein levels drives colinearity of gene order in metabolic operons of Escherichia coli. PLoS Biol. 2009, 7:e1000115.
    • (2009) PLoS Biol. , vol.7 , pp. e1000115
    • Kovács, K.1    Hurst, L.D.2    Papp, B.3
  • 12
    • 35748959334 scopus 로고    scopus 로고
    • PiQSi: protein quaternary structure investigation
    • Levy E.D. PiQSi: protein quaternary structure investigation. Structure 2007, 15:1364-1367.
    • (2007) Structure , vol.15 , pp. 1364-1367
    • Levy, E.D.1
  • 14
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • Li G.-W., Burkhardt D., Gross C., Weissman J.S. Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 2014, 157:624-635.
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.-W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 15
    • 79960614137 scopus 로고    scopus 로고
    • Fundamental relationship between operon organization and gene expression
    • Lim H.N., Lee Y., Hussein R. Fundamental relationship between operon organization and gene expression. Proc. Natl. Acad. Sci. USA 2011, 108:10626-10631.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10626-10631
    • Lim, H.N.1    Lee, Y.2    Hussein, R.3
  • 16
    • 84891765377 scopus 로고    scopus 로고
    • DOOR 2.0: presenting operons and their functions through dynamic and integrated views
    • Mao X., Ma Q., Zhou C., Chen X., Zhang H., Yang J., Mao F., Lai W., Xu Y. DOOR 2.0: presenting operons and their functions through dynamic and integrated views. Nucleic Acids Res. 2014, 42:D654-D659.
    • (2014) Nucleic Acids Res. , vol.42 , pp. D654-D659
    • Mao, X.1    Ma, Q.2    Zhou, C.3    Chen, X.4    Zhang, H.5    Yang, J.6    Mao, F.7    Lai, W.8    Xu, Y.9
  • 17
    • 84930715900 scopus 로고    scopus 로고
    • Structure, dynamics, assembly, and evolution of protein complexes
    • Marsh J.A., Teichmann S.A. Structure, dynamics, assembly, and evolution of protein complexes. Annu. Rev. Biochem. 2015, 84:551-575.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 551-575
    • Marsh, J.A.1    Teichmann, S.A.2
  • 19
    • 84938932863 scopus 로고    scopus 로고
    • Structural and evolutionary versatility in protein complexes with uneven stoichiometry
    • Marsh J.A., Rees H.A., Ahnert S.E., Teichmann S.A. Structural and evolutionary versatility in protein complexes with uneven stoichiometry. Nat. Commun. 2015, 6:6394.
    • (2015) Nat. Commun. , vol.6 , pp. 6394
    • Marsh, J.A.1    Rees, H.A.2    Ahnert, S.E.3    Teichmann, S.A.4
  • 20
    • 0030210340 scopus 로고    scopus 로고
    • Gene order is not conserved in bacterial evolution
    • Mushegian A.R., Koonin E.V. Gene order is not conserved in bacterial evolution. Trends Genet. 1996, 12:289-290.
    • (1996) Trends Genet. , vol.12 , pp. 289-290
    • Mushegian, A.R.1    Koonin, E.V.2
  • 21
    • 33847198656 scopus 로고    scopus 로고
    • Metabolic engineering of carotenoid biosynthesis in Escherichia coli by ordered gene assembly in Bacillus subtilis
    • Nishizaki T., Tsuge K., Itaya M., Doi N., Yanagawa H. Metabolic engineering of carotenoid biosynthesis in Escherichia coli by ordered gene assembly in Bacillus subtilis. Appl. Environ. Microbiol. 2007, 73:1355-1361.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1355-1361
    • Nishizaki, T.1    Tsuge, K.2    Itaya, M.3    Doi, N.4    Yanagawa, H.5
  • 22
    • 0019253694 scopus 로고
    • Translational coupling during expression of the tryptophan operon of Escherichia coli
    • Oppenheim D.S., Yanofsky C. Translational coupling during expression of the tryptophan operon of Escherichia coli. Genetics 1980, 95:785-795.
    • (1980) Genetics , vol.95 , pp. 785-795
    • Oppenheim, D.S.1    Yanofsky, C.2
  • 24
    • 84947221434 scopus 로고    scopus 로고
    • Operon structure and cotranslational subunit association direct protein assembly in bacteria
    • Shieh Y.-W., Minguez P., Bork P., Auburger J.J., Guilbride D.L., Kramer G., Bukau B. Operon structure and cotranslational subunit association direct protein assembly in bacteria. Science 2015, 350:678-680.
    • (2015) Science , vol.350 , pp. 678-680
    • Shieh, Y.-W.1    Minguez, P.2    Bork, P.3    Auburger, J.J.4    Guilbride, D.L.5    Kramer, G.6    Bukau, B.7
  • 25
    • 79952125361 scopus 로고    scopus 로고
    • Economy of operon formation: cotranscription minimizes shortfall in protein complexes
    • e00177-e10
    • Sneppen K., Pedersen S., Krishna S., Dodd I., Semsey S. Economy of operon formation: cotranscription minimizes shortfall in protein complexes. MBio 2010, 1. e00177-e10.
    • (2010) MBio , vol.1
    • Sneppen, K.1    Pedersen, S.2    Krishna, S.3    Dodd, I.4    Semsey, S.5
  • 26
    • 8544264562 scopus 로고    scopus 로고
    • Efficient attenuation of stochasticity in gene expression through post-transcriptional control
    • Swain P.S. Efficient attenuation of stochasticity in gene expression through post-transcriptional control. J. Mol. Biol. 2004, 344:965-976.
    • (2004) J. Mol. Biol. , vol.344 , pp. 965-976
    • Swain, P.S.1
  • 27
    • 0036790975 scopus 로고    scopus 로고
    • Intrinsic and extrinsic contributions to stochasticity in gene expression
    • Swain P.S., Elowitz M.B., Siggia E.D. Intrinsic and extrinsic contributions to stochasticity in gene expression. Proc. Natl. Acad. Sci. USA 2002, 99:12795-12800.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12795-12800
    • Swain, P.S.1    Elowitz, M.B.2    Siggia, E.D.3
  • 28
    • 23744515352 scopus 로고    scopus 로고
    • Mass spectrometry of the M. smegmatis proteome: protein expression levels correlate with function, operons, and codon bias
    • Wang R., Prince J.T., Marcotte E.M. Mass spectrometry of the M. smegmatis proteome: protein expression levels correlate with function, operons, and codon bias. Genome Res. 2005, 15:1118-1126.
    • (2005) Genome Res. , vol.15 , pp. 1118-1126
    • Wang, R.1    Prince, J.T.2    Marcotte, E.M.3
  • 29
    • 84941749221 scopus 로고    scopus 로고
    • Version 4.0 of PaxDb: Protein abundance data, integrated across model organisms, tissues, and cell-lines
    • Wang M., Herrmann C.J., Simonovic M., Szklarczyk D., von Mering C. Version 4.0 of PaxDb: Protein abundance data, integrated across model organisms, tissues, and cell-lines. Proteomics 2015, 15:3163-3168.
    • (2015) Proteomics , vol.15 , pp. 3163-3168
    • Wang, M.1    Herrmann, C.J.2    Simonovic, M.3    Szklarczyk, D.4    von Mering, C.5
  • 32
    • 33751190519 scopus 로고    scopus 로고
    • Optimal gene partition into operons correlates with gene functional order
    • Zaslaver A., Mayo A., Ronen M., Alon U. Optimal gene partition into operons correlates with gene functional order. Phys. Biol. 2006, 3:183-189.
    • (2006) Phys. Biol. , vol.3 , pp. 183-189
    • Zaslaver, A.1    Mayo, A.2    Ronen, M.3    Alon, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.