These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Cleavage of the lambda and P22 repressors by recA protein.
    Author: Sauer RT, Ross MJ, Ptashne M.
    Journal: J Biol Chem; 1982 Apr 25; 257(8):4458-62. PubMed ID: 6461657.
    Abstract:
    The site of recA cleavage of the phage lambda and P22 repressors has been determined. Each repressor is cut once by the recA enzyme, lambda repressor between residues 111 and 112, and P22 repressor between residues 94 and 95. recA cleavage occurs at identical alanyl-glycyl sequences in both repressors, and in both repressors, the cleavage separates the repressor's NH2-terminal DNA-binding domain from its COOH-terminal oligomerization domain. A papain-generated proteolytic fragment of lambda repressor consisting of repressor residues 93-236 is also efficiently cleaved by recA protein. Moreover, the recA cleavage of radioactive lambda repressor can be inhibited by certain COOH-terminal proteolytic fragments of lambda repressor which do not contain the alanyl-glycyl cleavage sequence. These facts suggest that recA cleavage of lambda repressor requires an intact COOH-terminal domain but not an intact NH2-terminal domain.
    [Abstract] [Full Text] [Related] [New Search]