一种嵌合Rec-A蛋白，其在同源配对中涉及非沃森-克里克相互作用。

A chimeric Rec-A protein that implicates non-Watson-Crick interactions in homologous pairing.

作者信息

Kurumizaka H, Rao B J, Ogawa T, Radding C M, Shibata T

机构信息

Laboratory of Cellular and Molecular Biology, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.

出版信息

Nucleic Acids Res. 1994 Aug 25;22(16):3387-91. doi: 10.1093/nar/22.16.3387.

DOI:10.1093/nar/22.16.3387

PMID:8078775

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC523733/

Abstract

The helical filament formed by RecA protein on single-stranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non-Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.

摘要

由RecA蛋白在单链DNA上形成的螺旋丝在同源重组中起重要作用，并与互补单链或同源双链DNA配对。RecA核蛋白丝也能识别相同的单链。嵌合蛋白RecAc38形成一种核蛋白丝，它能识别互补链，但在识别双链DNA方面存在缺陷，并与修复和重组中的表型缺陷有关。如本文所述，RecAc38核蛋白丝在识别相同链时也存在缺陷，无论该丝内部是单链还是双链DNA。一个假设存在三个DNA结合位点的模型使这些观察结果合理化，并表明第三个结合位点介导了非沃森-克里克相互作用，这些相互作用有助于识别双链DNA中的同源性。