The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyProgram in Molecular Medicine
Department of Cell Biology
Document Type
Journal ArticlePublication Date
1998-09-12Keywords
AcetatesAmino Acid Sequence
Animals
Catalysis
Cattle
Cyanogen Bromide
Cyclic AMP-Dependent Protein Kinases
Exons
Introns
Macromolecular Substances
Male
Molecular Sequence Data
Muscle, Skeletal
Myristic Acid
Peptide Fragments
Sequence Alignment
Sheep
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Sperm Head
Sperm Tail
Trypsin
Amino Acids, Peptides, and Proteins
Cell Biology
Cells
Enzymes and Coenzymes
Investigative Techniques
Urogenital System
Metadata
Show full item recordAbstract
The basis for the unusual properties of the catalytic subunit (C) of ram sperm cAMP-dependent protein kinase was investigated. Ram sperm C was purified and found by mass spectrometry (MS) to be approximately 890 Da smaller than Calpha, the predominant somatic isoform. Partial internal amino acid sequence from ram sperm C was an exact match to that of bovine Calpha, but differed from the predicted sequences for the Cbeta and Cgamma isoforms. MS analysis of 2-nitro-5-thiocyanatobenzoic acid fragments showed that the mass difference originated in the amino-terminal region. A unique blocked amino-terminal fragment was isolated from sperm C and sequenced by a combination of tandem mass spectrometry and Edman degradation of a subfragment. The results revealed that the amino-terminal myristate and the first 14 amino acids of Calpha are replaced by an amino-terminal acetate and six different amino acids in sperm C. The predicted mass difference due to these changes is 899 Da. The region of homology between sperm C and Calpha begins at the exon 1/exon 2 boundary in Calpha, suggesting that sperm C results from use of an alternate exon 1 in the Calpha gene. The different amino terminus of sperm C may be related to a unique requirement for localization of the "free" C subunit within the sperm flagellum.Source
J Biol Chem. 1998 Sep 18;273(38):24874-83.
DOI
10.1074/jbc.273.38.24874Permanent Link to this Item
http://hdl.handle.net/20.500.14038/26519PubMed ID
9733793Related Resources
ae974a485f413a2113503eed53cd6c53
10.1074/jbc.273.38.24874