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The human SETMAR protein preserves most of the activities of the ancestral Hsmar1 transposase.

Abstract：

:Transposons have contributed protein coding sequences to a unexpectedly large number of human genes. Except for the V(D)J recombinase and telomerase, all remain of unknown function. Here we investigate the activity of the human SETMAR protein, a highly expressed fusion between a histone H3 methylase and a mariner family transposase. Although SETMAR has demonstrated methylase activity and a DNA repair phenotype, its mode of action and the role of the transposase domain remain obscure. As a starting point to address this problem, we have dissected the activity of the transposase domain in the context of the full-length protein and the isolated transposase domain. Complete transposition of an engineered Hsmar1 transposon by the transposase domain was detected, although the extent of the reaction was limited by a severe defect for cleavage at the 3' ends of the element. Despite this problem, SETMAR retains robust activity for the other stages of the Hsmar1 transposition reaction, namely, site-specific DNA binding to the transposon ends, assembly of a paired-ends complex, cleavage of the 5' end of the element in Mn(2+), and integration at a TA dinucleotide target site. SETMAR is unlikely to catalyze transposition in the human genome, although the nicking activity may have a role in the DNA repair phenotype. The key activity for the mariner domain is therefore the robust DNA-binding and looping activity which has a high potential for targeting the histone methylase domain to the many thousands of specific binding sites in the human genome provided by copies of the Hsmar1 transposon.

journal_name

Mol Cell Biol

journal_title

Molecular and cellular biology

authors

Liu D,Bischerour J,Siddique A,Buisine N,Bigot Y,Chalmers R

doi

10.1128/MCB.01899-06

subject

Has Abstract

pub_date

2007-02-01 00:00:00

pages

1125-32

issue

3

eissn

0270-7306

issn

1098-5549

pii

MCB.01899-06

journal_volume

27

pub_type

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