The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo.
The endonuclease Ankle1 requires its LEM and GIY-YIG motifs for DNA cleavage in vivo.
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DOI:
10.1242/jcs.098392
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发表时间:
2012-02-15
影响因子:
4
通讯作者:
Foisner R
中科院分区:
文献类型:
--
作者:
Brachner A;Braun J;Ghodgaonkar M;Castor D;Zlopasa L;Ehrlich V;Jiricny J;Gotzmann J;Knasmüller S;Foisner R
The Lamina-associated polypeptide, Emerin, MAN1 - (LEM) domain defines a group of nuclear proteins, which bind chromatin through interaction of the LEM motif with the conserved DNA cross-linking protein, Barrier-to-Auto-Integration factor (BAF). Here, we describe a novel LEM protein, annotated in databases as “Ankyrin 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. While most characterized LEM proteins are components of the inner nuclear membrane, ectopic Ankle1 shuttles between cytoplasm and nucleus, and 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 represents a novel LEM-protein with a GIY-YIG type endonuclease activity in higher eukaryotes.
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影响因子:
64.5
作者:
Fekairi S;Scaglione S;Chahwan C;Taylor ER;Tissier A;Coulon S;Dong MQ;Ruse C;Yates JR 3rd;Russell P;Fuchs RP;McGowan CH;Gaillard PHL
通讯作者:
Gaillard PHL
影响因子:
11.4
作者:
Cai, ML;Huang, Y;Clore, GM
通讯作者:
Clore, GM
影响因子:
4
作者:
Dechat, T;Gajewski, A;Foisner, R
通讯作者:
Foisner, R
影响因子:
4.8
作者:
Holaska, JM;Lee, KK;Wilson, KL
通讯作者:
Wilson, KL
DOI:
10.1073/pnas.88.17.7719
发表时间:
1991-09-01
影响因子:
11.1
作者:
BELLPEDERSEN, D;QUIRK, SM;BELFORT, M
通讯作者:
BELFORT, M