Thumbnail
Access Restriction
Open

Author Menetski, Joseph P. ♦ Varghese, Abraham ♦ Kowalczykowskij, Stephen C.
Source CiteSeerX
Content type Text
File Format PDF
Subject Domain (in DDC) Computer science, information & general works ♦ Data processing & computer science
Subject Keyword Escherichia Coli ♦ Enzymatic Property ♦ Protein Display Anion-specific Inhibition ♦ Single-stranded Dna ♦ M13 Ssdna ♦ Reduced Rate ♦ Joint Molecule Formation ♦ Whereas Concentration ♦ Sodium Glutamate ♦ Reca Protein ♦ Atp Hy-drolysis ♦ Complete Inhibition ♦ Complete Exchange ♦ Dna-depend-ent Atpase ♦ Ionic Composition ♦ Dependent Atpase Activity ♦ Naglu Concentration ♦ Coli Ssdna ♦ Enzymatic Activity ♦ Dna Strand Exchange ♦ Dna Strand
Abstract The enzymatic activities of Escherichia coli recA protein are sensitive to ionic composition. Here we report that sodium glutamate (NaGlu) is much less inhibitory to the DNA strand exchange, DNA-depend-ent ATPase, and DNA binding activities of the recA protein than is NaC1. Both joint molecule formation and complete exchange of DNA strands occur (albeit at reduced rates) at NaGlu concentrations as high as 0.5 M whereas concentrations of NaCl greater than 0.2 M are sufficient for complete inhibition. The single-stranded DNA (ssDNA)-dependent ATPase activity is even less sensitive to inhibition by NaGlu; ATP hy-drolysis stimulated by M13 ssDNA is unaffected by 0.6 M NaGlu and is further stimulated by E. coli ssDNA binding protein-2-fold. Finally, NaGlu has essentially
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Research
Education Level UG and PG ♦ Career/Technical Study