Study on Biological Activity of Various Truncations of Human PRMT5 in E.coli
- VernacularTitle:对大肠杆菌中表达蛋白质精氨酸甲基转移酶5的几个缺失突变体的活性研究
- Author:
Litao SUN
;
Zhongwei ZHOU
;
Xiaodong XIE
;
Shilai BAO
- Publication Type:Journal Article
- Keywords:
PRMT5;
expression;
purification;
methyltransferases activity
- From:
Progress in Biochemistry and Biophysics
2008;35(7):801-806
- CountryChina
- Language:Chinese
-
Abstract:
Protein arginine methyltransferase 5 (PRMT5) has been implicated as an important regulator of many cellular processes and signaling pathways,including chromatin remodeling,RNA splicing,DNA transcription,and cell proliferation.Therefore,structural and functional studies on PRMT5 are quite important.The full length ofPRMT5 gene was cloned into vector pGEX-4T-1,resulting in only low expression levels in Escherichia coli (E.colO.Here,it was showed that the several N-terminal amino acids deletions could result in a significant increase in the amount of soluble ft"action,while one of them did not affect the protein-arginine methyltransferase activity.And it was also found that the N-terminal 15 amino acids region of PRMT5 may be important for the catalytic activity.
