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Distinct CG and CNG DNA methyltransferases in Pisum sativum

Distinct CG and CNG DNA methyltransferases in Pisum sativum DNA methyltransferase activity, present in low salt extracts of nuclei from young pea shoot apices, has been fractionated into two different species by assaying with model substrates. The CG methyltransferase (an unstable enzyme believed to be of 140 kDa) methylates cytosine only in oligonucleotides with CG and CI dinucleotide targets while an enzyme of 110 kDa (the CNG methyltransferase) methylates the cytosines in 5′‐CAG‐3′ and 5′‐CTG‐3′ target sequences, especially when hemimethylated, but not in 5′‐CCG‐3′ nor in 5′‐CGG‐3′ target sequences present in oligonucleotides. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Plant Journal Wiley

Distinct CG and CNG DNA methyltransferases in Pisum sativum

The Plant Journal , Volume 7 (3) – Mar 1, 1995

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Publisher
Wiley
Copyright
Copyright © 1995 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0960-7412
eISSN
1365-313X
DOI
10.1046/j.1365-313X.1995.7030471.x
Publisher site
See Article on Publisher Site

Abstract

DNA methyltransferase activity, present in low salt extracts of nuclei from young pea shoot apices, has been fractionated into two different species by assaying with model substrates. The CG methyltransferase (an unstable enzyme believed to be of 140 kDa) methylates cytosine only in oligonucleotides with CG and CI dinucleotide targets while an enzyme of 110 kDa (the CNG methyltransferase) methylates the cytosines in 5′‐CAG‐3′ and 5′‐CTG‐3′ target sequences, especially when hemimethylated, but not in 5′‐CCG‐3′ nor in 5′‐CGG‐3′ target sequences present in oligonucleotides.

Journal

The Plant JournalWiley

Published: Mar 1, 1995

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