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哺乳动物聚腺苷酸聚合酶的突变分析确定了一个与X家族聚合酶及其他核苷酸转移酶同源的引物结合区域和催化结构域。

Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases.

作者信息

Martin G, Keller W

机构信息

Department of Cell Biology, University of Basel, Basel, Switzerland.

出版信息

EMBO J. 1996 May 15;15(10):2593-603.

PMID:8665867
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC450192/
Abstract

We have tested deletion and substitution mutants of bovine poly(A) polymerase, and have identified a small region that overlaps with a nuclear localization signal and binds to the RNA primer. Systematic mutagenesis of carboxylic amino acids led to the identification of three aspartates that are essential for catalysis. Sequence and secondary structure comparisons of regions surrounding these aspartates with sequences of other polymerases revealed a significant homology to the palm structure of DNA polymerase beta, terminal deoxynucleotidyltransferase and DNA polymerase IV of Saccharomyces cerevisiae, all members of the family X of polymerases. This homology extends as far as cca: tRNA nucleotidyltransferase and streptomycin adenylyltransferase, an antibiotic resistance factor.

摘要

我们对牛多聚腺苷酸聚合酶的缺失和替代突变体进行了测试,并确定了一个与核定位信号重叠且能与RNA引物结合的小区域。对羧基氨基酸进行系统诱变后,鉴定出了三个对催化作用至关重要的天冬氨酸。将这些天冬氨酸周围区域的序列和二级结构与其他聚合酶的序列进行比较,发现其与DNA聚合酶β、末端脱氧核苷酸转移酶以及酿酒酵母DNA聚合酶IV(均为X家族聚合酶成员)的掌状结构具有显著同源性。这种同源性一直延伸到cca:tRNA核苷酸转移酶和链霉素腺苷酸转移酶(一种抗生素抗性因子)。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/ace0a246abcf/emboj00010-0280-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/a5140f718391/emboj00010-0274-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/ffa984242121/emboj00010-0275-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/62342c17362a/emboj00010-0276-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/1b92f74b5a53/emboj00010-0276-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/5b2f98aab95c/emboj00010-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/a1d7ea9e382c/emboj00010-0278-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/ace0a246abcf/emboj00010-0280-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/a5140f718391/emboj00010-0274-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/ffa984242121/emboj00010-0275-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/62342c17362a/emboj00010-0276-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/1b92f74b5a53/emboj00010-0276-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/5b2f98aab95c/emboj00010-0277-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/a1d7ea9e382c/emboj00010-0278-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab13/450192/ace0a246abcf/emboj00010-0280-a.jpg

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