Structural and Functional Studies of H. seropedicae RecA Protein – Insights into the Polymerization of RecA Protein as Nucleoprotein Filament

Leite, Wellington C.; Galvão, Carolina W.; Saab, Sérgio C.; Iulek, Jorge; Etto, Rafael M.; Steffens, Maria B. R.; Chitteni-Pattu, Sindhu; Stanage, Tyler; Keck, James L.; Cox, Michael M.; Spies, Maria

doi:10.1371/journal.pone.0159871

Title: Structural and Functional Studies of H. seropedicae RecA Protein – Insights into the Polymerization of RecA Protein as Nucleoprotein Filament

Journal Article · Fri Jul 22 00:00:00 EDT 2016 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0159871· OSTI ID:1347027

^[1]; Galvão, Carolina W. ^[1]; Saab, Sérgio C. ^[1]; Iulek, Jorge ^[1]; Etto, Rafael M. ^[1]; Steffens, Maria B. R. ^[2]; Chitteni-Pattu, Sindhu ^[3]; Stanage, Tyler ^[3]; Keck, James L. ^[3]; Cox, Michael M. ^[3]; Spies, Maria ^[4]

Ponta Grossa State Univ. (UEPG), PR (Brazil)
Federal Univ. of Parana, Curitiba (Brazil)
Univ. of Wisconsin, Madison, WI (United States)
Univ. of Iowa, Iowa City, IA (United States)

The bacterial RecA protein plays a role in the complex system of DNA damage repair. Here, we report the functional and structural characterization of the Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more efficient at displacing SSB protein from ssDNA than Escherichia coli RecA protein. HsRecA also promotes DNA strand exchange more efficiently. The three dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 Å resolution. HsRecA protein contains a small N-terminal domain, a central core ATPase domain and a large C-terminal domain, that are similar to homologous bacterial RecA proteins. Comparative structural analysis showed that the N-terminal polymerization motif of archaeal and eukaryotic RecA family proteins are also present in bacterial RecAs. Reconstruction of electrostatic potential from the hexameric structure of HsRecA-ADP/ATP revealed a high positive charge along the inner side, where ssDNA is bound inside the filament. The properties of this surface may explain the greater capacity of HsRecA protein to bind ssDNA, forming a contiguous nucleoprotein filament, displace SSB and promote DNA exchange relative to EcRecA. In conclusion, our functional and structural analyses provide insight into the molecular mechanisms of polymerization of bacterial RecA as a helical nucleoprotein filament.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: INCT-FBN; National Inst. of General Medical Sciences (NIGMS)

Grant/Contract Number:: GM098885; GM32335

OSTI ID:: 1347027

Journal Information:: PLoS ONE, Vol. 11, Issue 7; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 6 works

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Title: Structural and Functional Studies of H. seropedicae RecA Protein – Insights into the Polymerization of RecA Protein as Nucleoprotein Filament

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