期刊
FEBS LETTERS
卷 585, 期 5, 页码 809-813出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.02.007
关键词
CCCH Zn-finger; mRNA turnover; Smr domain; RNA endonuclease; Ubiquitination; Leishmania donovani
资金
- Department of Biotechnology, Govt. of India [BT/PR8139/BRB/10/519/2006]
- Department of Atomic Energy, Govt. of India [MMDDA-11-RD-SIN-5.04]
In trypanosomatid parasites, an octanucleotide sequence (C/A)AUAGAA(G/A) in the UTRs primarily determines the stability of S-phase specific mRNAs. A multi-domain protein LdCSBP from Leishmania donovani interacts with the UTR of an S-phase RNA containing the octanucleotide sequence through its unique CCCH-type Zn-finger motifs. Interestingly, the RNA binding protein contains a previously characterized DNA endonuclease domain - Smr. It has been demonstrated here that the LdCSBP Smr domain independently possesses both DNA and RNA endonuclease activities, but the full-length LdCSBP exhibits only riboendonuclease activity. Moreover, LdCSBP protein has been shown to be ubiquitinated, resulting in the down-regulation of its riboendonuclease activity. In conclusion, the results described here suggest a novel regulatory mechanism of mRNA degradation through ubiquitination in eukaryotes. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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