Titre :

Expression of a nonmyristylated variant of the catalytic subunit of protein kinase A during male germ-cell development.

Auteur(s) :

Desseyn, Jean-Luc [Auteur]
Lille Inflammation Research International Center - U 995 [LIRIC]
Burton, K A [Auteur]
McKnight, G S [Auteur]

Titre de la revue :

Proceedings of the National Academy of Sciences of the United States of America

Nom court de la revue :

Proc Natl Acad Sci U S A

Numéro :

97

Pagination :

6433-8

Date de publication :

2000-06-06

ISSN :

0027-8424

Mot(s)-clé(s) en anglais :

Alternative Splicing
Amino Acid Sequence
Animals
Base Sequence
Catalytic Domain
Chromosome Mapping
Conserved Sequence
Cyclic AMP-Dependent Protein Kinases
Enzyme Activation
Humans
Isoenzymes
Male
Mice
Mice
Inbred C57BL
Molecular Sequence Data
Spermatozoa
Testis
Transcription
Genetic

Discipline(s) HAL :

Sciences du Vivant [q-bio]

Résumé en anglais : [en]

The catalytic subunits of protein kinase A are transcribed in all mouse tissues from two distinct genes that code for the Calpha and Cbeta isoforms. Alternative promoters exist for the Cbeta gene that are used in a ...
Lire la suite >The catalytic subunits of protein kinase A are transcribed in all mouse tissues from two distinct genes that code for the Calpha and Cbeta isoforms. Alternative promoters exist for the Cbeta gene that are used in a tissue-specific fashion and give rise to variants that differ in their amino-terminal sequences. We have characterized an alternative promoter that is present in the first intron of the Calpha gene and is transcriptionally active in male germ cells. Transcription from this promoter is coincident with the appearance of pachytene spermatocytes and leads to a Calpha protein (Calpha2) that contains a distinctive 7 amino acid amino-terminus differing from the 14 amino acid amino-terminus of Calpha1. The Calpha2 protein does not contain the myristylation signal present on Calpha1 and migrates at a lower molecular weight on SDS/PAGE gels. By Western blotting, we estimate that most or all of the Calpha protein present in mature sperm is Calpha2. The amino-terminal sequence of Calpha2 is similar to that of ovine sperm C as previously reported [San Agustin, J. T., Leszyk, J. D., Nuwaysir, L. M. & Witman, G. B. (1998) J. Biol. Chem. 273, 24874-24883], and we show by cDNA cloning that human sperm also express a highly related Calpha2 homolog. The Calpha2 subunit forms holoenzymes with either RIIalpha or RIalpha, and both activate at the same concentration of cyclic nucleotide. Because protein kinase A is thought to play a pivotal role in sperm motility and capacitation, the distinctive biochemical properties of the unmyristylated Calpha2 may be essential for fertility in the male.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Collections :

• Institut de Recherche Translationnelle sur l'Inflammation (INFINITE) - U1286

Date de dépôt :

2019-07-09T09:08:25Z
2019-07-09T09:49:24Z