Direct Monitoring of Allosteric Recognition of Type IIE Restriction Endonuclease EcoRII
نویسندگان
چکیده
منابع مشابه
Asymmetric photocross-linking pattern of restriction endonuclease EcoRII to the DNA recognition sequence.
The EcoRII homodimer engages two of its recognition sequences (5'-CCWGG) simultaneously and is therefore a type IIE restriction endonuclease. To identify the amino acids of EcoRII that interact specifically with the recognition sequence, we photocross-linked EcoRII with oligonucleotide substrates that contained only one recognition sequence for EcoRII. In this recognition sequence, we substitut...
متن کاملEvolutionary relationship between different subgroups of restriction endonucleases.
The type II restriction endonuclease SsoII shows sequence similarity with 10 other restriction endonucleases, among them the type IIE restriction endonuclease EcoRII, which requires binding to an effector site for efficient DNA cleavage, and the type IIF restriction endonuclease NgoMIV, which is active as a homotetramer and cleaves DNA with two recognition sites in a concerted reaction. We show...
متن کاملSequence determination of restriction-endonuclease recognition sites.
the enzyme DpnII, produced by another strain of D. pneumoniae, recognizes the same sequence, but is inhibited by this same methylated base. The significance of the occurrence of modified nucleotides in eukaryotic DNA is not as yet understood, although a relationship between modification and gene expression has been proposed by several workers (Waalwijk & Flavell, 1978; Bird et al., 1979). By us...
متن کاملUbaLAI is a monomeric Type IIE restriction enzyme
Type II restriction endonucleases (REases) form a large and highly diverse group of enzymes. Even REases specific for a common recognition site often vary in their oligomeric structure, domain organization and DNA cleavage mechanisms. Here we report biochemical and structural characterization of the monomeric restriction endonuclease UbaLAI, specific for the pseudosymmetric DNA sequence 5'-CC/W...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m800334200