Crystal-Structure of the Hhai DNA Methyltransferase

Cheng, X., Kumar, S., Klimasauskas, S., Roberts, R. J. (June 1993) Crystal-Structure of the Hhai DNA Methyltransferase. Cold Spring Harb Symp Quant Biol, 58. pp. 331-338. ISSN 0091-7451

URL: http://www.ncbi.nlm.nih.gov/pubmed/7956046
DOI: 10.1101/SQB.1993.058.01.039

Abstract

DNA methyltransferases (MTases) exist in diverse organisms ranging from bacteria to mammals (Adams 1990). As a component of restriction and modification systems in bacteria, MTases methylate the DNA of the host cell and protect it from degradation by the cognate endonuclease, whose main function is believed to be the destruction of foreign DNA (Roberts and Halford 1993). Among type II restriction and modification systems, MTases recognize specifically four to eight base pairs of DNA, usually in palindromic sequences where methylation occurs symmetrically (Roberts and Halford 1993). MTases require S-adenosyl-L-methionine (AdoMet) as their methyl donor and act mainly as monomers. Because a fairly large number of MTases with diverse specificities are available, they offer exceptional opportunities for understanding how enzymes recognize and modify DNA.

Item Type: Paper
Uncontrolled Keywords: TARGET-RECOGNIZING DOMAINS ESCHERICHIA-COLI DETERMINES METHYLATION CATALYTIC MECHANISM MAMMALIAN NUCLEI SEQUENCE MOTIFS MET REPRESSOR BINDING EXPRESSION PROTEIN
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > methyltransferase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > restriction enzyme
CSHL Authors:
Communities: CSHL labs > Roberts lab
Depositing User: Matt Covey
Date: June 1993
Date Deposited: 21 Apr 2016 16:34
Last Modified: 21 Apr 2016 16:34
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32500

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