CONSERVATION OF COMPLEX DNA RECOGNITION DOMAINS BETWEEN FAMILIES OF RESTRICTION ENZYMES
CONSERVATION OF COMPLEX DNA RECOGNITION DOMAINS BETWEEN FAMILIES OF RESTRICTION ENZYMES
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DOI:
10.1016/0092-8674(89)90988-4
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发表时间:
1989-01-13
期刊:
影响因子:
64.5
通讯作者:
MURRAY, NE
中科院分区:
文献类型:
--
作者:
COWAN, GM;GANN, AAF;MURRAY, NE
One polypeptide, designated S, confers sequence-specificity to the multisubunit type I restriction enzymes. Two families of such enzymes, K and A, include members that recognize diverse, bipartite, target sequences. The S polypeptides of the K family, while having areas of near identity, also contain two extensive regions of variable sequence. We now show that one of these, comprising the N-terminal 150 amino acids, specifies recognition of one component of the bipartite target sequence. We have determined the sequence recognized by EcoE, a member of the A family. This sequence, 5''GAG(N7)ATGC, has the trinucleotide GAG in common with EcoA and with StySB of the K family. We determined the nucleotide sequences of the S genes of EcoA and EcoE, and compared their predicted amino acid sequences with each other and with those of the five members of the K family. There is no general sequence similarity between families, but the domain of the S polypeptide of StySB, which specifies GAG, shows nearly 50 percent identity with the amino variable region of the S polypeptides of EcoA and EcoE. A complex domain that recognizes and directs methylation of GAG is therefore common to enzymes of generally dissimilar amino acid sequence.