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The Sea Urchin Stem-loop-binding Protein: a Maternally Expressed Protein That Probably Functions in Expression of Multiple Classes of Histone MRNA

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Specialty Biochemistry
Date 2004 Feb 6
PMID 14762208
Citations 6
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Abstract

Following the completion of oogenesis and oocyte maturation, histone mRNAs are synthesized and stored in the sea urchin egg pronucleus. Histone mRNAs are the only mRNAs that are not polyadenylated but instead end in a stem-loop which has been conserved in evolution. The 3' end binds the stem-loop-binding protein (SLBP), and SLBP is required for histone pre-mRNA processing as well as translation of the histone mRNAs. A cDNA encoding a 59 kDa sea urchin SLBP (suSLBP) has been cloned from an oocyte cDNA library. The suSLBP contains an RNA-binding domain that is similar to the RNA-binding domain found in SLBPs from other species, although there is no similarity between the rest of the suSLBP and other SLBPs. The suSLBP is present at constant levels in eggs and for the first 12 h of development. The levels of suSLBP then decline and remain at a low level for the rest of embryogenesis. The suSLBP is concentrated in the egg pronucleus and is released from the nucleus only when cells enter the first mitosis. SuSLBP expressed by in vitro translation does not bind the stem-loop RNA, suggesting that suSLBP is modified to activate RNA binding in sea urchin embryos.

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References
1.
Wang Z, Ingledue T, Dominski Z, Sanchez R, Marzluff W . Two Xenopus proteins that bind the 3' end of histone mRNA: implications for translational control of histone synthesis during oogenesis. Mol Cell Biol. 1998; 19(1):835-45. PMC: 83940. DOI: 10.1128/MCB.19.1.835. View

2.
Martin F, Schaller A, Eglite S, Schumperli D, Muller B . The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein. EMBO J. 1997; 16(4):769-78. PMC: 1169678. DOI: 10.1093/emboj/16.4.769. View

3.
Dominski Z, Marzluff W . Formation of the 3' end of histone mRNA. Gene. 1999; 239(1):1-14. DOI: 10.1016/s0378-1119(99)00367-4. View

4.
Cameron C, Garey J, Swalla B . Evolution of the chordate body plan: new insights from phylogenetic analyses of deuterostome phyla. Proc Natl Acad Sci U S A. 2000; 97(9):4469-74. PMC: 18258. DOI: 10.1073/pnas.97.9.4469. View

5.
Whitfield M, Zheng L, Baldwin A, Ohta T, Hurt M, Marzluff W . Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol Cell Biol. 2000; 20(12):4188-98. PMC: 85788. DOI: 10.1128/MCB.20.12.4188-4198.2000. View