Structure, function, and mechanism of HhaI DNA methyltransferases

Umesh T. Sankpal; Desirazu N. Rao

doi:10.1080/10409230290771492

Structure, function, and mechanism of HhaI DNA methyltransferases

Umesh T. Sankpal, Desirazu N. Rao

Research output: Contribution to journal › Review article › peer-review

28 Scopus citations

Abstract

A vast amount of literature has accumulated on the characterization of DNA methyltransferases. The HhaI DNA methyltransferase, a C5-cytosine methyltransferase, has been the subject of investigation for the last 2 decades. Biochemical and kinetic characterization have led to an understanding of the catalytic and kinetic mechanism of the methyltransfer reaction. The HhaI methyltransferase has also been subjected to extensive structural analysis, with the availability of 12 structures with or without a cofactor and a variety of DNA substrates. The mechanism of base flipping, first described for the HhaI methyltransferase, is conserved among all DNA methyltransferases and is also found to occur in numerous DNA repair enzymes. Studies with other methyltransferase reveal a significant structural and functional similarity among different types of methyltransferases. This review aims to summarize the available information on the HhaI DNA methyltransferase.

Original language	English
Pages (from-to)	167-197
Number of pages	31
Journal	Critical Reviews in Biochemistry and Molecular Biology
Volume	37
Issue number	3
DOIs	https://doi.org/10.1080/10409230290771492
State	Published - 2002

Keywords

Base flipping
C5-cytosine DNA methyltransferases
DNA methylation
HhaI methyltransferase

Access to Document

10.1080/10409230290771492

Cite this

@article{c1a28c9931c9473ca4801874148349f9,

title = "Structure, function, and mechanism of HhaI DNA methyltransferases",

abstract = "A vast amount of literature has accumulated on the characterization of DNA methyltransferases. The HhaI DNA methyltransferase, a C5-cytosine methyltransferase, has been the subject of investigation for the last 2 decades. Biochemical and kinetic characterization have led to an understanding of the catalytic and kinetic mechanism of the methyltransfer reaction. The HhaI methyltransferase has also been subjected to extensive structural analysis, with the availability of 12 structures with or without a cofactor and a variety of DNA substrates. The mechanism of base flipping, first described for the HhaI methyltransferase, is conserved among all DNA methyltransferases and is also found to occur in numerous DNA repair enzymes. Studies with other methyltransferase reveal a significant structural and functional similarity among different types of methyltransferases. This review aims to summarize the available information on the HhaI DNA methyltransferase.",

keywords = "Base flipping, C5-cytosine DNA methyltransferases, DNA methylation, HhaI methyltransferase",

author = "Sankpal, {Umesh T.} and Rao, {Desirazu N.}",

note = "Funding Information: Work on HhaI DNA methyltransferase in our laboratory was supported by a research grant from DBT, Government of India. We thank Rich Roberts and New England Biolabs, USA, for all the help and support. D.N.R. thanks the Rockefeller Foundation, USA, for the award of the Biotechnology Career Award Fellowship.",

year = "2002",

doi = "10.1080/10409230290771492",

language = "English",

volume = "37",

pages = "167--197",

journal = "Critical Reviews in Biochemistry and Molecular Biology",

issn = "1040-9238",

publisher = "Informa Healthcare",

number = "3",

}

TY - JOUR

T1 - Structure, function, and mechanism of HhaI DNA methyltransferases

AU - Sankpal, Umesh T.

AU - Rao, Desirazu N.

N1 - Funding Information: Work on HhaI DNA methyltransferase in our laboratory was supported by a research grant from DBT, Government of India. We thank Rich Roberts and New England Biolabs, USA, for all the help and support. D.N.R. thanks the Rockefeller Foundation, USA, for the award of the Biotechnology Career Award Fellowship.

PY - 2002

Y1 - 2002

N2 - A vast amount of literature has accumulated on the characterization of DNA methyltransferases. The HhaI DNA methyltransferase, a C5-cytosine methyltransferase, has been the subject of investigation for the last 2 decades. Biochemical and kinetic characterization have led to an understanding of the catalytic and kinetic mechanism of the methyltransfer reaction. The HhaI methyltransferase has also been subjected to extensive structural analysis, with the availability of 12 structures with or without a cofactor and a variety of DNA substrates. The mechanism of base flipping, first described for the HhaI methyltransferase, is conserved among all DNA methyltransferases and is also found to occur in numerous DNA repair enzymes. Studies with other methyltransferase reveal a significant structural and functional similarity among different types of methyltransferases. This review aims to summarize the available information on the HhaI DNA methyltransferase.

AB - A vast amount of literature has accumulated on the characterization of DNA methyltransferases. The HhaI DNA methyltransferase, a C5-cytosine methyltransferase, has been the subject of investigation for the last 2 decades. Biochemical and kinetic characterization have led to an understanding of the catalytic and kinetic mechanism of the methyltransfer reaction. The HhaI methyltransferase has also been subjected to extensive structural analysis, with the availability of 12 structures with or without a cofactor and a variety of DNA substrates. The mechanism of base flipping, first described for the HhaI methyltransferase, is conserved among all DNA methyltransferases and is also found to occur in numerous DNA repair enzymes. Studies with other methyltransferase reveal a significant structural and functional similarity among different types of methyltransferases. This review aims to summarize the available information on the HhaI DNA methyltransferase.

KW - Base flipping

KW - C5-cytosine DNA methyltransferases

KW - DNA methylation

KW - HhaI methyltransferase

UR - http://www.scopus.com/inward/record.url?scp=0036063744&partnerID=8YFLogxK

U2 - 10.1080/10409230290771492

DO - 10.1080/10409230290771492

M3 - Review article

C2 - 12139442

AN - SCOPUS:0036063744

SN - 1040-9238

VL - 37

SP - 167

EP - 197

JO - Critical Reviews in Biochemistry and Molecular Biology

JF - Critical Reviews in Biochemistry and Molecular Biology

IS - 3

ER -

Structure, function, and mechanism of HhaI DNA methyltransferases

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this