DSpace

Digital.CSIC > Biología y Biomedicina > Centro de Biología Molecular Severo Ochoa (CBM) > (CBM) Artículos >

Share

EndNote

Impact

Links

Closed Access item The in vivo function of phage φ29 nucleoid-associated protein p6 requires formation of dimers

Authors:Abril, Ana M.
Salas, Margarita
Hermoso, José Miguel
Keywords:Bacillus subtilis, In vivo crosslinking, Protein–protein interaction, DNA replication
Issue Date:21-Aug-2002
Publisher:Elsevier
Citation:Gene 296(1-2): 187-194 (2002)
Abstract:The Bacillus subtilis phage φ29 nucleoid-associated protein p6 (103 amino acids) is essential for in vivo viral DNA replication and control of transcription, and it has been proposed to play a role in genome organization and compaction. This protein self-associates in vitro from preformed dimers forming high-molecular-weight oligomers and binds to double-stranded DNA giving rise to multimeric nucleoprotein complexes. Site-directed mutants, p6I8T and p6A44V, were completely or partially inactive, respectively, in an in vitro dimerization assay. In this paper, and by in vivo crosslinking, we have detected dimers of protein p6 either in phage-infected cells or in protein p6 producing B. subtilis or Escherichia coli cells. Therefore, this self-association does not require viral DNA. We also show that mutants p6I8T and p6A44V are deficient in dimer formation, and they do not support phage DNA replication in a trans-complementation assay with φ29sus6 mutant-infected B. subtilis cells. We conclude that dimeric protein p6 is the active form of the protein in vivo, required for viral DNA replication.
Publisher version (URL):http://dx.doi.org/10.1016/S0378-1119(02)00857-0
URI:http://hdl.handle.net/10261/39362
ISSN:0378-1119
???metadata.dc.identifier.doi???:10.1016/S0378-1119(02)00857-0
Appears in Collections:(CBM) Artículos

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.