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
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: | https://repository.cshl.edu/id/eprint/32500 |
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