The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Stem-Loop Binding Protein, the Protein That Binds the 3′ End of Histone mRNA, Is Cell Cycle Regulated by Both Translational and Posttranslational Mechanisms
Open accessAbstract
The expression of the replication-dependent histone mRNAs is tightly regulated during the cell cycle. As cells progress from G(1) to S phase, histone mRNA levels increase 35-fold, and they decrease again during G(2) phase. Replication-dependent histone mRNAs are the only metazoan mRNAs that lack polyadenylated tails, ending instead in a conserved stem-loop. Much of the cell cycle regulation is posttranscriptional and is mediated by the 3' stem-loop. A 31-kDa stem-loop binding protein (SLBP) binds the 3' end of histone mRNA. The SLBP is necessary for pre-mRNA processing and accompanies the histone mRNA to the cytoplasm, where it is a component of the histone messenger RNP. We used synchronous CHO cells selected by mitotic shakeoff and HeLa cells synchronized at the G(1)/S or the M/G(1) boundary to study the regulation of SLBP during the cell cycle. In each system the amount of SLBP is regulated during the cell cycle, increasing 10- to 20-fold in the late G(1) and then decreasing in the S/G(2) border. SLBP mRNA levels are constant during the cell cycle. SLBP is regulated at the level of translation as cells progress from G(1) to S phase, and the protein is rapidly degraded as they progress into G(2). Regulation of SLBP may account for the posttranscriptional component of the cell cycle regulation of histone mRNA.
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Citations
Cites
How Proteolysis Drives the Cell Cycle
King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273
Cited by
Whitfield, M. L., Sherlock, G., Saldanha, A. J., Murray, J. I., Ball, C. A., Alexander, K. E., Matese, J. C., Perou, C. M., Hurt, M. M., Brown, P. O., et al. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-02-0030 · Cited by 1,527
Self-citationMethylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 865
Regulation of mRNA stability in mammalian cells
Guhaniyogi, J., & Brewer, G. (2001) · Gene · doi:10.1016/s0378-1119(01)00350-x · Cited by 729
Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin
Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 663
Reduced histone biosynthesis and chromatin changes arising from a damage signal at telomeres
O'Sullivan, R. J., Kubicek, S., Schreiber, S. L., & Karlseder, J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1897 · Cited by 416
Metadata
- Authors
- Whitfield, M. L., Zheng, L.-X., Baldwin, A., Ohta, T., Hurt, M. M., & Marzluff, W. F.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2000-06
- Volume
- 20
- Issue
- 12
- Pages
- 4188-4198
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2130418521
- Cited by
- 248
- References
- 1
- FWCI
- 3.49
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Stem-Loop Binding Protein, the Protein That Binds the 3′ End of Histone mRNA, Is Cell Cycle Regulated by Both Translational and Posttranslational Mechanisms. https://app.cochat.ai/papers/10.1128/mcb.20.12.4188-4198.2000
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- Whitfield, M. L., Zheng, L.-X., Baldwin, A., Ohta, T., Hurt, M. M., & Marzluff, W. F. (2000). Stem-Loop Binding Protein, the Protein That Binds the 3′ End of Histone mRNA, Is Cell Cycle Regulated by Both Translational and Posttranslational Mechanisms. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.20.12.4188-4198.2000
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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