Artigo Acesso aberto Revisado por pares

A leucine zipper motif determines different functions in a DNA replication protein.

1996; Springer Nature; Volume: 15; Issue: 4 Linguagem: Inglês

10.1002/j.1460-2075.1996.tb00427.x

ISSN

1460-2075

Autores

Darı́o Garcı́a de Viedma, Rafael Giraldo, Germán Rivas, Elena Fernández-Tresguerres, Ramón Díaz‐Orejas,

Tópico(s)

RNA modifications and cancer

Resumo

Research Article15 February 1996free access A leucine zipper motif determines different functions in a DNA replication protein. D. Garcia de Viedma D. Garcia de Viedma Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author R. Giraldo R. Giraldo Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author G. Rivas G. Rivas Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author E. Fernández-Tresguerres E. Fernández-Tresguerres Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author R. Diaz-Orejas R. Diaz-Orejas Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author D. Garcia de Viedma D. Garcia de Viedma Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author R. Giraldo R. Giraldo Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author G. Rivas G. Rivas Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author E. Fernández-Tresguerres E. Fernández-Tresguerres Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author R. Diaz-Orejas R. Diaz-Orejas Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. Search for more papers by this author Author Information D. Garcia de Viedma1, R. Giraldo1, G. Rivas1, E. Fernández-Tresguerres1 and R. Diaz-Orejas1 1Departamento de Microbiologia Molecular, Centro de Investigaciones Biologicas, Madrid, Spain. The EMBO Journal (1996)15:925-934https://doi.org/10.1002/j.1460-2075.1996.tb00427.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info RepA is the replication initiator protein of the Pseudomonas plasmid pPS10 and is also able to autoregulate its own synthesis. Here we report a genetic and functional analysis of a leucine zipper-like (LZ) motif located at the N-terminus of RepA. It is shown that the LZ motif modulates the equilibrium between monomeric and dimeric forms of the protein and that monomers of RepA interact with sequences at the origin of replication, oriV, while dimers are required for interactions of RepA at the repA promoter. Further, different residues of the LZ motif are seen to have different functional roles. Leucines at the d positions of the putative alpha-helix are relevant in the formation of RepA dimers required for transcriptional autoregulation. They also modulate other RepA-RepA interactions that result in cooperative binding of protein monomers to the origin of replication. The residues at the b/f positions of the putative helix play no relevant role in RepA-RepA interactions. These residues do not affect RepA autoregulation but do influence replication, as demonstrated by mutants that, without affecting binding to oriV, either increase the host range of the plasmid or are inactive in replication. It is proposed that residues in b/f positions play a relevant role in interactions between RepA and host replication factors. Previous ArticleNext Article Volume 15Issue 41 February 1996In this issue RelatedDetailsLoading ...

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