CLONING OF THE LARGE SUBUNIT OF ACTIVATOR-1 (REPLICATION FACTOR-C) REVEALS HOMOLOGY WITH BACTERIAL-DNA LIGASES

被引：63

作者：

BURBELO, PD ^{[1
]}

UTANI, A ^{[1
]}

PAN, ZQ ^{[1
]}

YAMADA, Y ^{[1
]}

机构：

[1] MEM SLOAN KETTERING CANC RES CTR,SLOAN KETTERING INST,PROGRAM MOLEC BIOL,NEW YORK,NY 10021

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 24期

关键词：

DNA REPLICATION; ACCESSORY PROTEINS; DNA-BINDING PROTEIN;

D O I：

10.1073/pnas.90.24.11543

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We have cloned a gene encoding a DNA-binding protein by Southwestern screening of a murine cDNA library with a double-stranded oligonucleotide containing the sequence from the bidirectional promoter of the alpha1 and alpha2 collagen IV genes. The middle portion of this 1131-amino acid protein has a region homologous to bacterial DNA ligases, and the more carboxyl portion contains several domains homologous to p40, p38, p37, and p36.5 subunits of activator 1 (A1, also called replication factor C), a human replication protein complex. Western blotting revealed that antiserum generated against part of the recombinant protein reacted specifically with the 145-kDa component of the purified human A1 complex, indicating that it is the murine counterpart of the A1 p145. Characterization of the DNA-binding activity of the recombinant fusion protein by gel mobility-shift assay revealed that it had a preference for a run of pyrimidines on one strand. Deletion analysis using recombinant proteins revealed that the DNA ligase-like domain was required for DNA-binding activity. The finding that the region required for the binding of murine A1 p145 to DNA has similarity to a domain found in DNA ligases suggests that this region may be utilized by both proteins in recognizing DNA.

引用

页码：11543 / 11547

页数：5

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