DnaB解旋酶与DnaI装载蛋白结构相互作用的研究进展
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摘要
DNA复制是生命现象最本质的内容,由众多蛋白共同参与的能确保遗传信息精确及时传递的复杂的生物学过程。目前对DNA复制起始及其调控的分子机制了解还不很清楚。通过对研究解旋酶DnaB及装载蛋白DnaI的文献调研,希望有助于人们进一步了解DNA复制起始的一系列复杂过程。此外,研究DnaB与DnaI的相互抑制作用,也可为后续细菌抗生素的研究奠定基础,是新一代抗生素的研究方向之一。
DNA replication is the most essential content of life phenomena, and it is a complicated biological process involving many proteins to ensure accurate and timely transmission of genetic information. At present, the molecular mechanism of DNA replication initiation and its regulation is still unclear. Through the literature research on the helicase DnaB and the loaded protein DnaI it is hoped that it will help people to further understand a series of complicated processes of DNA replication initiation. In addition, the study of the mutual inhibition between DnaB and DnaI can also lay a foundation for the subsequent study of bacterial antibiotics, which is one of the research directions of the new generation of antibiotics.
DNA replication is the most essential content of life phenomena, and it is a complicated biological process involving many proteins to ensure accurate and timely transmission of genetic information. At present, the molecular mechanism of DNA replication initiation and its regulation is still unclear. Through the literature research on the helicase DnaB and the loaded protein DnaI it is hoped that it will help people to further understand a series of complicated processes of DNA replication initiation. In addition, the study of the mutual inhibition between DnaB and DnaI can also lay a foundation for the subsequent study of bacterial antibiotics, which is one of the research directions of the new generation of antibiotics.
引文
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[7]Nakayama N,Arai N,Kaziro Y,et al.Structural and functional studies of the DnaB protein using limited proteolysis.Characterization of domains for DNA-dependent ATPhydrolysis and for protein association in the primosome[J].Journal of Biological Chemistry,1984,259(1):88-96.
[8]Bailey S,Eliason W K,Steitz T A.Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase[J].Science,2007,318(5849):459-463.
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[10]Lo Y H,Tsai K L,Sun Y J,et al.The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA[J].Nucleic Acids Research,2009,37(3):804-814.
[11]Wang,G.,Klein,M.G.,Tokonzaba,E.,Zhang,Y.,Holden,L.G.,and Chen,X.S.The structure of a DnaB-family replicative helicase and its interactions with primase[J].Nat.Struct.Mol.Biol,2008,15,94-100.
[12]Soultanas,P..Loading mechanisms of ring helicases at replication origins[J].Mol.Microbiol,2012,84,6-16.
[13]Biswas,S.B.,Flowers,S.,and Biswas-Fiss,E.E.Quantitative analysis of nucleotide modulation of DNA binding by DnaCprotein of Escherichia coli[J].Biochem.J,2004,379,553-562.
[14]Liu,B.,W.K.Eliason,and T.A.Steitz..Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly[J].Nat Commun,2013,4:p.2495.
[15]Hood I V,Berger J M.Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication[J].Elife,2016,5.
[16]Davey M J,O'Donnell M.Replicative helicase loaders:ring breakers and ring makers.[J].Current Biology,2003,13(15):R594-R596.
[2]Li,Y.and H.Araki,Loading and activation of DNAreplicative helicases:the key step of initiation of DNAreplication.Genes Cells,2013.18(4):p.266-77.
[3]Lebowitz,J.H.and R.Mcmacken,The Escherichia-Coli Dnab Replication Protein Is a DNA Helicase.Journal of Biological Chemistry,1986.261(10):p.4738-4748.
[4]Biswas,S.B.,P.H.Chen,and E.E.Biswas,Structure and Function of Escherichia-Coli Dnab Protein-Role of the N-Terminal Domain in Helicase Activity.Biochemistry,1994.33(37):p.11307-11314.
[5]Bailey,S.,W.K.Eliason,and T.A.Steitz,Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase.Science,2007.318(5849):p.459-463.
[6]Barcena,M.,et al.,The DnaB.DnaC complex:a structure based on dimers assembled around an occluded channel.EMBOJ,2001.20(6):p.1462-8.
[7]Nakayama N,Arai N,Kaziro Y,et al.Structural and functional studies of the DnaB protein using limited proteolysis.Characterization of domains for DNA-dependent ATPhydrolysis and for protein association in the primosome[J].Journal of Biological Chemistry,1984,259(1):88-96.
[8]Bailey S,Eliason W K,Steitz T A.Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase[J].Science,2007,318(5849):459-463.
[9]Strycharska M S,Ariaspalomo E,Lyubimov A Y,et al.Nucleotide and partner-protein control of bacterial replicative helicase structure and function.[J].Molecular Cell,2013,52(6):844-854.
[10]Lo Y H,Tsai K L,Sun Y J,et al.The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA[J].Nucleic Acids Research,2009,37(3):804-814.
[11]Wang,G.,Klein,M.G.,Tokonzaba,E.,Zhang,Y.,Holden,L.G.,and Chen,X.S.The structure of a DnaB-family replicative helicase and its interactions with primase[J].Nat.Struct.Mol.Biol,2008,15,94-100.
[12]Soultanas,P..Loading mechanisms of ring helicases at replication origins[J].Mol.Microbiol,2012,84,6-16.
[13]Biswas,S.B.,Flowers,S.,and Biswas-Fiss,E.E.Quantitative analysis of nucleotide modulation of DNA binding by DnaCprotein of Escherichia coli[J].Biochem.J,2004,379,553-562.
[14]Liu,B.,W.K.Eliason,and T.A.Steitz..Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly[J].Nat Commun,2013,4:p.2495.
[15]Hood I V,Berger J M.Viral hijacking of a replicative helicase loader and its implications for helicase loading control and phage replication[J].Elife,2016,5.
[16]Davey M J,O'Donnell M.Replicative helicase loaders:ring breakers and ring makers.[J].Current Biology,2003,13(15):R594-R596.
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