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Ubiquitination of mRNA cycling sequence binding protein from Leishmania donovani (LdCSBP) modulates the RNA endonuclease activity of its Smr domain
Author(s) -
Bhandari Dipankar,
Guha Kasturi,
Bhaduri Nipa,
Saha Partha
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.02.007
Subject(s) - endonuclease , rna , rna binding protein , biology , messenger rna , microbiology and biotechnology , untranslated region , ubiquitin , dna , genetics , gene
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.