mRNA cycling sequence binding protein from Leishmania donovani (LdCSBP) is covalently modified by ubiquitination
| Autor: | Partha Saha, Dipankar Bhandari |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Untranslated region
Regulation of gene expression Ubiquitin binding Ubiquitin Binding protein Amino Acid Motifs Molecular Sequence Data Protozoan Proteins RNA RNA-Binding Proteins Biology Ubiquitin-conjugating enzyme Microbiology Molecular biology Cell biology Protein Structure Tertiary Gene Expression Regulation Gene expression Genetics Transcriptional regulation Animals RNA Processing Post-Transcriptional Molecular Biology Sequence Alignment Leishmania donovani |
| Zdroj: | FEMS microbiology letters. 273(2) |
| ISSN: | 0378-1097 |
| Popis: | The lack of transcriptional regulation in trypanosomatids suggests the presence of distinct posttranscriptional mechanisms to control differential gene expression. In fact, the stability of S-phase specific mRNAs in these parasites is determined primarily by the presence of the octanucleotide sequence (C/A)AUAGAA(G/A) in the UTRs of the transcripts. Here, the characterization of LdCSBP is reported, which specifically binds to the octanucleotide containing RNA. The LdCSBP protein contains multiple putative functional domains, including two types of ubiquitin binding domains (UBA and CUE), two CCCH-type Zn-finger motifs probably responsible for specific RNA binding activity and a speculative endonuclease domain SMR. Interestingly, the protein is covalently modified through ubiquitination. This observation and the occurrence of multiple ubiquitin binding domains in the protein raise the possibility of regulation of the activity of LdCSBP by ubiquitination. |
| Databáze: | OpenAIRE |
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