Conservation of complex DNA recognition domains between families of restriction enzymes

Cowan, G. M., Gann, A. A., Murray, N. E. (January 1989) Conservation of complex DNA recognition domains between families of restriction enzymes. Cell, 56 (1). pp. 103-9. ISSN 0092-8674 (Print)0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/2642743
DOI: 10.1016/0092-8674(89)90988-4

Abstract

One polypeptide, designated S, confers sequence-specificity to the multisubunit type I restriction enzymes. Two families of such enzymes, K and A, include members that recognize diverse, bipartite, target sequences. The S polypeptides of the K family, while having areas of near identity, also contain two extensive regions of variable sequence. We now show that one of these, comprising the N-terminal 150 amino acids, specifies recognition of one component of the bipartite target sequence. We have determined the sequence recognized by EcoE, a member of the A family. This sequence, 5'GAG(N7)ATGC, has the trinucleotide GAG in common with EcoA and with StySB of the K family. We determined the nucleotide sequences of the S genes of EcoA and EcoE, and compared their predicted amino acid sequences with each other and with those of the five members of the K family. There is no general sequence similarity between families, but the domain of the S polypeptide of StySB, which specifies GAG, shows nearly 50 per cent identity with the amino variable region of the S polypeptides of EcoA and EcoE. A complex domain that recognizes and directs methylation of GAG is therefore common to enzymes of generally dissimilar amino acid sequence.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence DNA Mutational Analysis DNA-Binding Proteins/*physiology Deoxyribonucleases, Type I Site-Specific/*physiology Escherichia coli/*enzymology Methylation Molecular Sequence Data Substrate Specificity
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > restriction enzyme
CSHL Authors:
Communities: Watson School
Depositing User: Matt Covey
Date: 13 January 1989
Date Deposited: 23 Jun 2014 19:23
Last Modified: 23 Jun 2014 19:23
Related URLs:
URI: http://repository.cshl.edu/id/eprint/30341

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