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水手Mos-1转座酶的ITR结合结构域。

The ITR binding domain of the Mariner Mos-1 transposase.

作者信息

Augé-Gouillou C, Hamelin M H, Demattei M V, Periquet G, Bigot Y

机构信息

IRBI Groupe d'Etude des Parasites Génétiques, URPESA CNRS 6035, Faculté des Sciences, Tours, France.

出版信息

Mol Genet Genomics. 2001 Mar;265(1):58-65. doi: 10.1007/s004380000386.

DOI:10.1007/s004380000386
PMID:11370873
Abstract

Mariner-like elements are widespread eukaryotic transposons, but Mos-1 is the only natural element that is known to be active. Little is known about the biochemistry of mariner transposition. The first step in the process is the binding of the transposase to the 5' and 3' inverted terminal repeats (ITRs) of the element. Using the 3' ITR of the element, we have determined the binding properties of a recombinant Mos-1 transposase produced in bacteria, and we have used deletion derivatives to localize the minimal ITR binding domain between amino acids 1 and 141. Its features and structure indicate that it differs from the ITR binding domain of the transposase encoded by Tc1-related elements.

摘要

类水手元件是广泛存在的真核转座子,但Mos-1是已知唯一具有活性的天然元件。关于水手转座的生物化学过程知之甚少。该过程的第一步是转座酶与元件的5'和3'反向末端重复序列(ITR)结合。利用该元件的3' ITR,我们确定了在细菌中产生的重组Mos-1转座酶的结合特性,并使用缺失衍生物将最小ITR结合域定位在氨基酸1至141之间。其特征和结构表明,它与Tc1相关元件编码的转座酶的ITR结合域不同。

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2
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