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J Biol Chem, Vol. 273, Issue 38, 24874-24883, September 18, 1998
From the 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 ~890 Da smaller than C
The Catalytic Subunit of the cAMP-dependent Protein
Kinase of Ovine Sperm Flagella Has a Unique Amino-terminal
Sequence
,
Department of Cell Biology and
§ Protein Chemistry Facility, University of Massachusetts
Medical Center, Worcester Foundation Campus, Shrewsbury, Massachusetts
01545 and ¶ Perkin Elmer Sciex, Applied Biosystems Division,
Foster City, California 94404
, the predominant
somatic isoform. Partial internal amino acid sequence from ram sperm C
was an exact match to that of bovine C, but differed from the
predicted sequences for the C
and C
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 C 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 C begins at the exon 1/exon 2 boundary in C,
suggesting that sperm C results from use of an alternate exon 1 in the
C 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.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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