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RNA RECOGNITION BY RNP PROTEINS DURING RNA PROCESSING
Abstract
▪ Abstract The ribonucleoprotein (RNP) domain is one of the most common eukaryotic protein folds. Proteins containing RNP domains function in important steps of posttranscriptional regulation of gene expression by directing the assembly of multiprotein complexes on primary transcripts, mature mRNAs, and stable ribonucleoprotein components of the RNA processing machinery. The diverse functions performed by these proteins depend on their dual ability to recognize RNA and to interact with other proteins, often utilizing specialized auxiliary domains. Crystallographic and NMR structures of several RNP domains and a handful of structures of RNA-protein complexes have begun to reveal the molecular basis for RNP-RNA recognition.
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Citations
Cited by
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Black, D. L. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161720 · Cited by 2,704
Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase
Jankowsky, E., Gross, C. H., Shuman, S., & Pyle, A. M. (2001) · Science · doi:10.1126/science.291.5501.121 · Cited by 305
Zakaryan, R. P., & Gehring, H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.08.018 · Cited by 98
Sequence requirements for RNA binding by HuR and AUF1
Barker, A., Epis, M. R., Porter, C. J., Hopkins, B. R., Wilce, M. C. J., Wilce, J. A., Giles, K. M., & Leedman, P. J. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs010 · Cited by 59
Metadata
- Authors
- Varani, G., & Nagai, K.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 1998-06
- Volume
- 27
- Issue
- 1
- Pages
- 407-445
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2112103350
- Cited by
- 300
- References
- 0
- FWCI
- 7.99
- Type
- journal article
- Language
- en
- Open access
- closed
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- Varani, G., & Nagai, K. (1998). RNA RECOGNITION BY RNP PROTEINS DURING RNA PROCESSING. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.27.1.407
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