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Predictive motifs derived from cytosine methyltransferases

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 hig... Full description

Journal Title: Nucleic Acids Research 1989, Vol.17(7), pp.2421-2435
Main Author: Pósfai, János
Other Authors: Bhagwat, Ashok S. , Pósfai, György , Roberts, Richard J.
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0305-1048 ; E-ISSN: 1362-4962 ; DOI: http://dx.doi.org/10.1093/nar/17.7.2421
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recordid: crossref10.1093/nar/17.7.2421
title: Predictive motifs derived from cytosine methyltransferases
format: Article
creator:
  • Pósfai, János
  • Bhagwat, Ashok S.
  • Pósfai, György
  • Roberts, Richard J.
subjects:
  • Chemistry
  • Anatomy & Physiology
ispartof: Nucleic Acids Research, 1989, Vol.17(7), pp.2421-2435
description: 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.
language: eng
source:
identifier: ISSN: 0305-1048 ; E-ISSN: 1362-4962 ; DOI: http://dx.doi.org/10.1093/nar/17.7.2421
fulltext: fulltext
issn:
  • 03051048
  • 0305-1048
  • 13624962
  • 1362-4962
url: Link


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descriptionThirteen 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.
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