Nucleic Acids Research, 1981, Vol. 9, No. 24 6795-6804
© 1981
ENZYMOLOGY |
Purification and characterization of two new modification methylases; MClal from Caryophanon latum L and MTaqI from Thermus aquaticus YTI
Department of Molecular and Population Genetics, University of Georgia Athens, GA 30602, USA
Received September 25, 1981. A method for detecting Type II modification methylases and determining their methylation site by assaying the ability of methylated DNA to be cleaved by heterologous restriction enzymes is described and applied to the isolation of the restriction modification methylases from Thermus thermophilus HB8, Thermus aquaticus YTI and Caryophanon latum L. M.TaqI is shown to have a methylation specificity identical to M.TthI (TCGmeA). M.ClaI methylates at adenine and protects a subset of TthI sites indicating that it methylates the sequence ATCGmeAT. Methylation by M.TthI also protects against cleavage by SalI, XhoI and at some HindII, AccI and MboI sites.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
M. Watanabe, H. Yuzawa, N. Handa, and I. Kobayashi Hyperthermophilic DNA Methyltransferase M.PabI from the Archaeon Pyrococcus abyssi Appl. Envir. Microbiol., August 1, 2006; 72(8): 5367 - 5375. [Abstract] [Full Text] [PDF] |
||||
