Abstract：
: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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Brachner A,Braun J,Ghodgaonkar M,Castor D,Zlopasa L,Ehrlich V,Jiricny J,Gotzmann J,Knasmüller S,Foisner Rdoi
10.1242/jcs.098392subject
Has Abstractpub_date
2012-02-15 00:00:00pages
1048-57issue
Pt 4eissn
0021-9533issn
1477-9137pii
jcs.098392journal_volume
125pub_type
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