Predictive motifs derived from cytosine methyltransferases

Posfai, J., Bhagwat, A. S., Posfai, G., Roberts, R. J. (April 1989) Predictive motifs derived from cytosine methyltransferases. Nucleic Acids Res, 17 (7). pp. 2421-35. ISSN 0305-1048

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URL: http://www.ncbi.nlm.nih.gov/pubmed/2717398
DOI: 10.1093/nar/17.7.2421

Abstract

Thirteen bacterial DNA methyltransferases that catalyze the formation of 5-methylcytosine within specific DNA sequences possess related structures. Similar building blocks (motifs), containing invariant positions, can be found in the same order in all thirteen sequences. Five of these blocks are highly conserved while a further five contain weaker similarities. One block, which has the most invariant residues, contains the proline-cysteine dipeptide of the proposed catalytic site. A region in the second half of each sequence is unusually variable both in length and sequence composition. Those methyltransferases that exhibit significant homology in this region share common specificity in DNA recognition. The five highly conserved motifs can be used to discriminate the known 5-methylcytosine forming methyltransferases from all other methyltransferases of known sequence, and from all other identified proteins in the PIR, GenBank and EMBL databases. These five motifs occur in a mammalian methyltransferase responsible for the formation of 5-methylcytosine within CG dinucleotides. By searching the unidentified open reading frames present in the GenBank and EMBL databases, two potential 5-methylcytosine forming methyltransferases have been found.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Bacterial Proteins/genetics Catalysis Comparative Study *DNA (Cytosine-5-)-Methyltransferase/genetics Information Systems Molecular Sequence Data Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Sequence Homology, Nucleic Acid Software *Structure-Activity Relationship
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: 11 April 1989
Date Deposited: 26 Jun 2017 18:56
Last Modified: 08 Nov 2017 17:02
PMCID: PMC317633
Related URLs:
URI: http://repository.cshl.edu/id/eprint/34891

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