In:
Journal of Cell Science, The Company of Biologists, Vol. 125, No. 4 ( 2012-02-15), p. 1048-1057
Kurzfassung:
The LEM domain (for lamina-associated polypeptide, emerin, MAN1 domain) defines a group of nuclear proteins that bind chromatin through interaction of the LEM motif with the conserved DNA crosslinking protein, barrier-to-autointegration factor (BAF). Here, we describe a LEM protein annotated in databases as ‘Ankyrin repeat and LEM domain-containing protein 1’ (Ankle1). We show that Ankle1 is conserved in metazoans and contains a unique C-terminal GIY-YIG motif that confers endonuclease activity in vitro and in vivo. In mammals, Ankle1 is predominantly expressed in hematopoietic tissues. Although most characterized LEM proteins are components of the inner nuclear membrane, ectopic Ankle1 shuttles between cytoplasm and nucleus. Ankle1 enriched in the nucleoplasm induces DNA cleavage and DNA damage response. This activity requires both the catalytic C-terminal GIY-YIG domain and the LEM motif, which binds chromatin via BAF. Hence, Ankle1 is an unusual LEM protein with a GIY-YIG-type endonuclease activity in higher eukaryotes.
Materialart:
Online-Ressource
ISSN:
1477-9137
,
0021-9533
Sprache:
Englisch
Verlag:
The Company of Biologists
Publikationsdatum:
2012
ZDB Id:
219171-4
ZDB Id:
1483099-1
SSG:
12
