REPAIRtoire - a database of DNA repair pathways

Welcome! Click here to login or here to register.
Home
Proteins
DNA damage
Diseases
Homologs
Pathways
Keywords
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

"Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I."

Joyce CM, Kelley WS, Grindley ND



Published Jan. 25, 1982 in J Biol Chem volume 257 .

Pubmed ID: 6276402

Abstract:
We report the nucleotide sequence of 3.2 kilobase pair region of the Escherichia coli polA gene, comprising the coding region for DNA polymerase I with about 400 base pairs of flanking sequence. The amino acid sequence for DNA polymerase I derived from our DNA sequence is largely consistent with previous protein chemical data. In the following paper, Brown et al. (Brown, W. E., Stump, K. H., and Kelley, W. S. (1982) J. Biol. Chem. 257, 1965-1972) present additional protein chemistry experiments that further confirm our sequence. Mild proteolysis of DNA polymerase I is known to produce two enzymatically active fragments (Brutlag, D., Atkinson, M. R., Setlow, P., and Kornberg, A. (1969) Biochem. Biophys. Res. Commun. 37, 982-989; Klenow, H., and Henningsen, I. (1970) Proc. Natl. Acad. Sci. U. S. A. 74, 5632-5636). We have located the site of this cleavage between residues 323 and 324 of the 928 amino acid polymerase molecule. By sequence comparison of the polA1 and wild type alleles, we have identified the polA1 mutation as a change from Trp (TGG) to amber (TAG) at residue 342.


This publication refers to following REPAIRtoire entries:

Proteins


Last modification of this entry: Oct. 6, 2010

Add your own comment!

There is no comment yet.
Welcome stranger! Click here to login or here to register.
Valid HTML 4.01! This site is Emacs powered. Made with Django.