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PMID: 6983681 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Purification and properties of the Hpa I methylase.

Nucleic acids research ·Vol. 10 ·No. 20 ·1982-10-25 ·Pages 6511-9

Yoo OJ, Dwyer-Hallquist P, Agarwal KL

Abstract

The purification and catalytic properties of the homogeneous Hpa I methylase is described. The enzyme exists as a single polypeptide chain with a molecular weight of 37,000 +/- 2,000 was shown by sedimentation equilibrium and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The Hpa I methylase transfers methyl groups of S-adenosylmethionine to adenine present in the recognition sequence d(G-T-T-A-A*-C), A* is the N6 methyl adenosine. An average of 2.1 methyl groups per recognition site are transferred by the Hpa I methylase.

MeSH Terms
Haemophilus influenzae/enzymology Kinetics Methyltransferases/isolation & purification,metabolism Molecular Weight S-Adenosylmethionine Site-Specific DNA-Methyltransferase (Adenine-Specific) Substrate Specificity
Chemicals
S-Adenosylmethionine DNA modification methylase HpaI Methyltransferases Site-Specific DNA-Methyltransferase (Adenine-Specific)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Yoo O J
Dwyer-Hallquist P
Agarwal K L
References (11)
11 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/10.20.6511
Published
1982-10-25
Pages
6511-9
Language
English
Region
England
NLM ID
0411011
PMCID
PMC326940
Subset
IM
Grants
NIGMS NIH HHS · GM 22199 · United States
External Links
PubMed source DOI: 10.1093/nar/10.20.6511 PMC Full Text View journal details
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