4 results match your criteria pria helicase-deficient

  • Page 1 of 1

RecG Directs DNA Synthesis during Double-Strand Break Repair.

PLoS Genet 2016 Feb 12;12(2):e1005799. Epub 2016 Feb 12.

Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, United Kingdom.

Homologous recombination provides a mechanism of DNA double-strand break repair (DSBR) that requires an intact, homologous template for DNA synthesis. When DNA synthesis associated with DSBR is convergent, the broken DNA strands are replaced and repair is accurate. However, if divergent DNA synthesis is established, over-replication of flanking DNA may occur with deleterious consequences. Read More

View Article and Full-Text PDF
February 2016

Stringent response processes suppress DNA damage sensitivity caused by deficiency in full-length translation initiation factor 2 or PriA helicase.

Mol Microbiol 2014 Apr 28;92(1):28-46. Epub 2014 Feb 28.

Department of Biochemistry and Molecular & Cellular Biology, Georgetown University Medical Center, Box 571455, 3900 Reservoir Rd. NW, Washington, DC, 20057-1455, USA.

When Escherichia coli grows in the presence of DNA-damaging agents such as methyl methanesulphonate (MMS), absence of the full-length form of Translation Initiation Factor 2 (IF2-1) or deficiency in helicase activity of replication restart protein PriA leads to a considerable loss of viability. MMS sensitivity of these mutants was contingent on the stringent response alarmone (p)ppGpp being at low levels. While zero levels (ppGpp┬░) greatly aggravated sensitivity, high levels promoted resistance. Read More

View Article and Full-Text PDF

A new role for translation initiation factor 2 in maintaining genome integrity.

PLoS Genet 2012 19;8(4):e1002648. Epub 2012 Apr 19.

Department of Biochemistry and Molecular and Cellular Biology, Georgetown University Medical Center, Washington, DC, United States of America.

Escherichia coli translation initiation factor 2 (IF2) performs the unexpected function of promoting transition from recombination to replication during bacteriophage Mu transposition in vitro, leading to initiation by replication restart proteins. This function has suggested a role of IF2 in engaging cellular restart mechanisms and regulating the maintenance of genome integrity. To examine the potential effect of IF2 on restart mechanisms, we characterized its influence on cellular recovery following DNA damage by methyl methanesulfonate (MMS) and UV damage. Read More

View Article and Full-Text PDF
September 2012

Helicase-deficient cysteine to glycine substitution mutants of Escherichia coli replication protein PriA retain single-stranded DNA-dependent ATPase activity. Zn2+ stimulation of mutant PriA helicase and primosome assembly activities.

J Biol Chem 1993 Feb;268(6):4337-46

Program in Molecular Biology, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

The PriA replication protein of Escherichia coli guides the ordered assembly of the primosome, the mobile, multiprotein, bidirectional, DNA replication priming/helicase complex of which it is an integral part. Although the PriA protein is not essential for viability, primosome assembly via a PriA-dependent pathway is required for normal cellular replication and growth. The PriA protein itself is multifunctional. Read More

View Article and Full-Text PDF
February 1993
  • Page 1 of 1