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Regulation of histone mRNA in the unperturbed cell cycle: Evidence suggesting control at two posttranscriptional steps
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Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms
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This paper describes the cell-cycle regulation of SLBP, an essential protein for histone mRNA biosynthesis and stability. SLBP is likely the major protein responsible for coordinate cell cycle regulation of replication-dependent histone mRNAs in animal cells
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Whitfield M.L., Zheng L.X., Baldwin A., Ohta T., Hurt M.M., Marzluff W.F. 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. 20:2000;4188-4198. This paper describes the cell-cycle regulation of SLBP, an essential protein for histone mRNA biosynthesis and stability. SLBP is likely the major protein responsible for coordinate cell cycle regulation of replication-dependent histone mRNAs in animal cells.
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The gene for histone RNA hairpin binding protein is located on human chromosome 4 and encodes a novel type of RNA binding protein
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Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein
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This paper reports the identification of a novel Sm protein, which is an essential component of the U7 small nuclear ribonucleoprotein
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A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3′-end processing
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Using a novel extension of the yeast 3-hybrid system, the authors report the identification of a U7 snRNP protein that interacts with the SLBP-histone pre-mRNA complex
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Dominski Z., Erkmann J.A., Yang X., Sanchez R., Marzluff W.F. A novel zinc finger protein is associated with U7 snRNP and interacts with the stem-loop binding protein in the histone pre-mRNP to stimulate 3′-end processing. Genes Dev. 16:2002;58-71. Using a novel extension of the yeast 3-hybrid system, the authors report the identification of a U7 snRNP protein that interacts with the SLBP-histone pre-mRNA complex.
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The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro
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This paper provides direct evidence that SLBP stimulates translation of mRNAs containing a histone stem loop. SLBP only needs to be recruited to the 3' end of the mRNA, and does not need to be directly bound to the histone stem-loop to activate translation
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Sanchez R., Marzluff W.F. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol Cell Biol. 22:2002;7093-7104. This paper provides direct evidence that SLBP stimulates translation of mRNAs containing a histone stem loop. SLBP only needs to be recruited to the 3' end of the mRNA, and does not need to be directly bound to the histone stem-loop to activate translation.
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NPAT links cyclin E-cdk2 to the regulation of replication-dependent histone gene transcription
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Cell cycle-dependent localization of the CDK2-cyclin E complex in Cajal (coiled) bodies
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This paper demonstrates that in addition to NPAT, cyclin E-cdk2 is also present in Cajal bodies, implicating these proteins in cell-cycle regulation of histone gene transcription
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The stem-loop binding protein (SLBP1) is present in coiled bodies of the Xenopus germinal vesicle
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