title: SR protein-specific kinase 1 is highly expressed in testis and phosphorylates protamine 1.
abstract: Arginine/serine protein kinases constitute a novel class of enzymes that can modify arginine/serine (RS) dipeptide motifs. SR splicing factors that are essential for pre-mRNA splicing are among the best characterized proteins that contain RS domains. TwoSRprotein-specifickinases, SRPK1 and SRPK2, have been considered as highly specific for the phosphorylation of these proteins, thereby contributing to splicing regulation. However, despite the fact that SR proteins are more or less conserved among metazoa and have a rather ubiquitous tissue distribution we now demonstrate that SRPK1 is predominantly expressed in testis. In situ expression analysis on transverse sections of adult mouse testis shows that SRPK1 mRNA is abundant in all germinal cells but not in mature spermatozoa. RS kinase activity was found primarily in the cytosol and only minimal activity was detected in the nucleus. In a search for testis-specific substrates of SRPK1 we found that the enzyme phosphorylates human protamine 1 as well as a cytoplasmic pool of SR proteins present in the testis. Protamine 1 belongs to a family of small basic arginine-rich proteins that replace histones during the development of mature spermatozoa. The result of this progressive replacement is the formation of a highly compact chromatin structure devoid of any transcriptional activity. These findings indicate that SRPK1 may have a role not only in pre-mRNA splicing, but also in the condensation of sperm chromatin.
authors.affiliation: Laboratory of Biochemistry, School of Chemistry, The Aristotelian University of Thessaloniki, Thessaloniki 54 006, Greece.
authors.forename: S
authors.initials: S
authors.lastname: Papoutsopoulou
authors.forename: E
authors.initials: E
authors.lastname: Nikolakaki
authors.forename: G
authors.initials: G
authors.lastname: Chalepakis
authors.forename: V
authors.initials: V
authors.lastname: Kruft
authors.forename: P
authors.initials: P
authors.lastname: Chevaillier
authors.forename: T
authors.initials: T
authors.lastname: Giannakouros
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism; D009928:Organ Specificity; D010766:Phosphorylation; D011479:Protamines / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013094:Spermatozoa / Q000166:cytology / Q000378:metabolism; D013737:Testis / Q000166:cytology / Q000201:enzymology*
chemical_list: D009687:Nuclear Proteins; C082073:PRM1 protein, human; C513176:Prm1 protein, mouse; C513174:Prm1 protein, rat; D011479:Protamines; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins; C087728:SRPK1 protein, human; C490215:Srpk1 protein, mouse; D017346:Protein Serine-Threonine Kinases