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SR proteins[edit]
SR proteins are a conserved family of splicing proteins rich in alternating arginine and serine protein residues. SR proteins are important in constitutive and alternative pre-mRNA splicing and some post splicing activities of mRNA.[1] Proteins are classified as SR proteins if they have at least one RNA recognition motif (RRM) and one RS Domain.[1] Other qualification include recognition by the antibody mAb104 and purification using magnesium chloride.[1] In some cases a protein may lack the RRM domain, but is able to interact with RNA through other means. These proteins are called SR-related proteins.[1] SR proteins are localized to the nucleus of cells, specifically in nuclear speckles.[1]
SR proteins were discovered in the 1990's in Drosophila and around the same time in amphibian oocytes.[2][3] Further investigation has found SR proteins in humans.[1] In general, metazoans, multicellular organisms, appear to have SR proteins and unicellular organisms lack SR proteins.[4]
SR proteins have RNA recognition sites at N- and C-terminus arginine and serine rich sites.[5]
In plants it is thought that SR proteins play a role in development of specific tissues and responses to stress.[5] SR proteins also have a role in regulating post-splicing mRNA metabolism and general mRNA metabolism.[6]
SR proteins also bind to histone 3 tail to participate in transcriptional elongation to further organize gene expression not only at the RNA level, but also at the DNA level.[7]
References[edit]
- ^ a b c d e f Long, Jennifer C.; Caceres, Javier F. (2009 Jan 1). "The SR protein family of splicing factors: master regulators of gene expression". The Biochemical Journal. 417 (1): 15–27. doi:10.1042/BJ20081501. PMID 19061484.
{{cite journal}}: Check date values in:|date=(help)CS1 maint: date and year (link) - ^ Shepard, Peter J.; Hertel, Klemens J. (2009). "The SR protein family". Genome Biology. 10 (10): 242. doi:10.1186/gb-2009-10-10-242. PMC 2784316. PMID 19857271.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Zhong, Xiang-Yang; Wang, Pingping; Han, Joonhee; Rosenfeld, Michael G.; Fu, Xiang-Dong (2009 Jul 10). "SR proteins in vertical integration of gene expression from transcription to RNA processing to translation". Molecular Cell. 35 (1): 1–10. doi:10.1016/j.molcel.2009.06.016. PMC 2744344. PMID 19595711.
{{cite journal}}: Check date values in:|date=(help) - ^ Blencowe, BJ (1999). "SR-related proteins and the processing of messenger RNA precursors". Biochemistry and Cell Biology = Biochimie et Biologie Cellulaire. 77 (4): 277–91. doi:10.1139/o99-048. PMID 10546891.
{{cite journal}}: Unknown parameter|coauthors=ignored (|author=suggested) (help) - ^ a b Reddy, Anireddy S. N.; Shad Ali, Gul (1 November 2011). "Plant serine/arginine-rich proteins: roles in precursor messenger RNA splicing, plant development, and stress responses". Wiley Interdisciplinary Reviews: RNA. 2 (6): 875–889. doi:10.1002/wrna.98. PMID 21766458.
- ^ Shepard, P. J.; Hertel, K. J. (2009). "The SR protein family". Genome Biology. 10 (10): 242. doi:10.1186/gb-2009-10-10-242. PMC 2784316. PMID 19857271.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Zhong, Xiang-Yang; Wang, Pingping; Han, Joonhee; Rosenfeld, Michael G.; Fu, Xiang-Dong (2009). "SR Proteins in Vertical Integration of Gene Expression from Transcription to RNA Processing to Translation". Molecular Cell. 35 (1): 1–10. doi:10.1016/j.molcel.2009.06.016. PMC 2744344. PMID 19595711.