CONSERVATION OF ORGANIZATION IN THE SPECIFICITY POLYPEPTIDES OF 2 FAMILIES OF TYPE-I RESTRICTION ENZYMES
CONSERVATION OF ORGANIZATION IN THE SPECIFICITY POLYPEPTIDES OF 2 FAMILIES OF TYPE-I RESTRICTION ENZYMES
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DOI:
10.1016/0022-2836(89)90001-6
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发表时间:
1989-10-05
影响因子:
5.6
通讯作者:
MURRAY, NE
中科院分区:
文献类型:
--
作者:
KANNAN, P;COWAN, GM;MURRAY, NE
We have identified the recognition sequence for the Citrobacter freundii restriction endonuclease CfrA, a member of the A-family of type I R-M enzymes. This bipartite target sequence differs in both its components from those of other type I enzymes. We determined the nucleotide sequence of its specificity gene (hsdS) and a comparison of this with its relative EcoA identifies two extensive variable regions, an organization analogous to that found in the K-family of type I R-M enzymes. The specificity polypeptides of the A-family, unlike those of K, have an N-terminal conserved region, and this includes a sequence repeated within the central conserved region. A second repeat sequence, identified at the amino acid level, coincides with the only sequence similarity common to all types I S polypeptides. Sequences immediately downstream from the hsdS genes of EcoA, CfrA, EcoK, B and D are almost identical, consistent with an allelic chromosomal location.