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

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.

View Accepted Manuscript (DOE)

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

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

OSTI ID:: 1347027

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

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Macromolecular complexes in crystals and solutions Krissinel, Evgeny Acta Crystallographica Section D Biological Crystallography, Vol. 67, Issue 4 https://doi.org/10.1107/S0907444911007232	journal	March 2011
Structure of a hexameric form of RadA recombinase from Methanococcus voltae Du, Liqin; Luo, Yu Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 68, Issue 5 https://doi.org/10.1107/S1744309112010226	journal	April 2012
Evidence for Elongation of the Helical Pitch of the RecA Filament Upon ATP and ADP Binding Using Small-Angle Neutron Scattering Ellouze, Christine; Takahashi, Masayuki; Wittung, Pernilla European Journal of Biochemistry, Vol. 233, Issue 2 https://doi.org/10.1111/j.1432-1033.1995.579_2.x	journal	October 1995
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RecA Protein from the Extremely Radioresistant Bacterium Deinococcus radiodurans: Expression, Purification, and Characterization Kim, Jong-Il; Sharma, Ajay K.; Abbott, Stephen N. Journal of Bacteriology, Vol. 184, Issue 6 https://doi.org/10.1128/JB.184.6.1649-1660.2002	journal	March 2002
Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes Datta, S.; Krishna, R.; Ganesh, N. Journal of Bacteriology, Vol. 185, Issue 14 https://doi.org/10.1128/JB.185.14.4280-4284.2003	journal	July 2003
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Effects of various single-stranded-DNA-binding proteins on reactions promoted by RecA protein. Egner, C.; Azhderian, E.; Tsang, S. S. Journal of Bacteriology, Vol. 169, Issue 8 https://doi.org/10.1128/jb.169.8.3422-3428.1987	journal	January 1987
The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae Galvão, C. W.; Souza, E. M.; Etto, R. M. Brazilian Journal of Medical and Biological Research, Vol. 45, Issue 12 https://doi.org/10.1590/S0100-879X2012007500160	journal	December 2012
The RecX protein interacts with the RecA protein and modulates its activity in Herbaspirillum seropedicae Galvão, C. W.; Souza, E. M.; Etto, R. M. Brazilian Journal of Medical and Biological Research, Vol. 45, Issue 12 https://doi.org/10.1590/s0100-879x2012007500160	journal	December 2012

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MAW point mutation impairs H. Seropedicae RecA ATP hydrolysis and DNA repair without inducing large conformational changes in its structure Leite, Wellington C.; Penteado, Renato F.; Gomes, Fernando PLOS ONE, Vol. 14, Issue 4 https://doi.org/10.1371/journal.pone.0214601	journal	April 2019

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