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 react

SUBMITTER: Liu D 

PROVIDER: S-EPMC1800679 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature