Conservation of organization in the specificity polypeptides of two families of type I restriction enzymes

Kannan, P., Cowan, G. M., Daniel, A. S., Gann, A. A., Murray, N. E. (October 1989) Conservation of organization in the specificity polypeptides of two families of type I restriction enzymes. Journal of Molecular Biology, 209 (3). pp. 335-44. ISSN 0022-2836 (Print)0022-2836

Abstract

We have identified the recognition sequence for the Citrobacter freundii restriction endonuclease CfrA, a member of the A-family of type I R-M enzymes. This bipartite target sequence differs in both its components from those of other type I enzymes. We determined the nucleotide sequence of its specificity gene (hsdS) and a comparison of this with its relative EcoA identifies two extensive variable regions, an organization analogous to that found in the K-family of type I R-M enzymes. The specificity polypeptides of the A-family, unlike those of K, have an N-terminal conserved region, and this includes a sequence repeated within the central conserved region. A second repeat sequence, identified at the amino acid level, coincides with the only sequence similarity common to all type I S polypeptides. Sequences immediately downstream from the hsdS genes of EcoA, CfrA, EcoK, B and D are almost identical, consistent with an allelic chromosomal location.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Base Sequence Citrobacter/*enzymology Codon DNA, Bacterial Deoxyribonucleases, Type I Site-Specific/*genetics Genes, Bacterial Molecular Sequence Data Peptides/*genetics Repetitive Sequences, Nucleic Acid
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > restriction enzyme
CSHL Authors:
Communities: School of Biological Sciences > SBS Administration
Depositing User: Matt Covey
Date: 5 October 1989
Date Deposited: 23 Jun 2014 19:21
Last Modified: 09 Sep 2021 18:53
Related URLs:
URI: https://repository.cshl.edu/id/eprint/30340

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