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cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding
Alain Lescure1, Christine Allmang, Kenichiro Yamada
1UPR 9002 du Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 15, Rue René Descartes, 67084 Strasbourg Cedex, France.
Gene
|July 4, 2002
Summary
Human selenocysteine insertion sequence binding protein (SBP2) is crucial for selenoprotein synthesis. Its binding to SECIS RNA is enhanced by the translation factor mSelB/eEFsec, highlighting a key step in mammalian selenoprotein production.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Selenocysteine and selenoprotein synthesis involve intricate molecular machinery in mammals.
- A key component is the RNA-protein complex of selenocysteine insertion sequence (SECIS) binding protein (SBP2) and the SECIS element RNA hairpin.
Purpose of the Study:
- To isolate and characterize human SBP2 complementary DNA (cDNA).
- To compare human SBP2 with a previously reported SBP2-like protein.
- To investigate the expression pattern and functional interactions of human SBP2.
Main Methods:
- Isolation of human SBP2 cDNA.
- Sequence comparison between human and rat SBP2.
- Analysis of human SBP2 mRNA expression patterns.
- Investigation of human SBP2 binding to SECIS RNA, including the role of mSelB/eEFsec.
Main Results:
- Human SBP2 cDNA was isolated, confirming it differs from a previously reported SBP2-like protein.
- Human SBP2 is encoded by a 4 kb mRNA, over-expressed in testis.
- Highly conserved domains (92% and 95% identity) were identified in human SBP2 compared to rat SBP2, with one domain containing the RNA binding site.
- Human SBP2 binding to SECIS RNA is stimulated by the selenoprotein-specialized translation factor mSelB/eEFsec.
Conclusions:
- Human SBP2 is a distinct protein involved in selenoprotein synthesis.
- SBP2 expression is prominent in the testis.
- The interaction between SBP2 and SECIS RNA is regulated by mSelB/eEFsec, providing new insights into selenoprotein translation regulation.