PMID- 10390541
OWN - NLM
STAT- MEDLINE
DCOM- 19990903
LR  - 20190501
IS  - 0305-1048 (Print)
IS  - 0305-1048 (Linking)
VI  - 27
IP  - 14
DP  - 1999 Jul 15
TI  - SR protein-specific kinase 1 is highly expressed in testis and phosphorylates
      protamine 1.
PG  - 2972-80
AB  - 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.
FAU - Papoutsopoulou, S
AU  - Papoutsopoulou S
AD  - Laboratory of Biochemistry, School of Chemistry, The Aristotelian University of
      Thessaloniki, Thessaloniki 54 006, Greece.
FAU - Nikolakaki, E
AU  - Nikolakaki E
FAU - Chalepakis, G
AU  - Chalepakis G
FAU - Kruft, V
AU  - Kruft V
FAU - Chevaillier, P
AU  - Chevaillier P
FAU - Giannakouros, T
AU  - Giannakouros T
LA  - eng
SI  - GENBANK/AJ224115
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nucleic Acids Res
JT  - Nucleic acids research
JID - 0411011
RN  - 0 (Nuclear Proteins)
RN  - 0 (PRM1 protein, human)
RN  - 0 (Prm1 protein, mouse)
RN  - 0 (Prm1 protein, rat)
RN  - 0 (Protamines)
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - EC 2.7.1.- (SRPK1 protein, human)
RN  - EC 2.7.1.- (Srpk1 protein, mouse)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Cloning, Molecular
MH  - HeLa Cells
MH  - Humans
MH  - Kinetics
MH  - Male
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Nuclear Proteins/metabolism
MH  - Organ Specificity
MH  - Phosphorylation
MH  - Protamines/*metabolism
MH  - Protein-Serine-Threonine Kinases/chemistry/*genetics/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Recombinant Fusion Proteins/chemistry/genetics/metabolism
MH  - Spermatozoa/cytology/metabolism
MH  - Testis/cytology/*enzymology
PMC - PMC148514
EDAT- 1999/07/03 00:00
MHDA- 1999/07/03 00:01
CRDT- 1999/07/03 00:00
PHST- 1999/07/03 00:00 [pubmed]
PHST- 1999/07/03 00:01 [medline]
PHST- 1999/07/03 00:00 [entrez]
AID - gkc443 [pii]
AID - 10.1093/nar/27.14.2972 [doi]
PST - ppublish
SO  - Nucleic Acids Res. 1999 Jul 15;27(14):2972-80. doi: 10.1093/nar/27.14.2972.