An Uncommon Multiphosphorylated Lipid in Neurospora-Crassa Whose Formation Is Catalyzed Invitro by a Calcium-Dependent and Phospholipid-Dependent Kinase

Détails

ID Serval
serval:BIB_33B2C885B6BF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
An Uncommon Multiphosphorylated Lipid in Neurospora-Crassa Whose Formation Is Catalyzed Invitro by a Calcium-Dependent and Phospholipid-Dependent Kinase
Périodique
Plant Science
Auteur(s)
Favre  B., Mauco  G., Turian  G., Chap  H.
ISSN
0168-9452
Statut éditorial
Publié
Date de publication
1991
Peer-reviewed
Oui
Volume
77
Numéro
1
Pages
67-80
Notes
Gc754
Times Cited:2
Cited References Count:37
Résumé
The presence of a calcium- and phospholipid-dependent kinase activity in the soluble extracts of Neurospora crassa has been reported earlier. This activity phosphorylated in vitro two endogenous substrates, one of apparent molecular weight (M(r)) 85 000, the other much lower than 14 000. This paper reports that the smaller substrate is a lipid. The lower M(r) phosphorylated compound could be extracted from proteins by organic solvents. Various thin-layer chromatographic analyses revealed that it did not comigrate with any of the phospholipids tested. Chemical and enzymatic structural analyses indicated that the phosphorylated compound was sensitive to mild alkaline methanolysis, alkaline phosphatase and phospholipase A1 but resistant to phospholipases A2, C and D or nitrous acid treatment. A similar compound was detected in the organic phase after extraction of N. crassa mycelia labelled in vivo with either (P(i))-P-32 or [H-3]glycerol. It could not be detected when [H-3]inositol was used as label. The addition of in vivo P-32-labelled lipids in phosphorylation reactions revealed that the low M(r) substrate of the calcium- and phospholipid-dependent kinase already contained some phosphate which was itself sensitive to alkaline phosphatase. An identical apolar component was generated by alkaline phosphatase treatment of both the substrate of the kinase and the phosphorylated substrate. From these data it is concluded that the low M(r) phosphorylated compound is a lipid, presumably consisting of a diacylglycerol backbone with an as yet undetermined structure linked to the glycerol moiety. This structure contains at least two phosphate groups.
Mots-clé
kinase phosphorylation phospholipid calcium-dependent enzyme phospholipid-dependent enzyme neurospora-crassa cellular-regulation proteins cells identification rat membrane vesicles family brain
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Création de la notice
25/01/2008 17:32
Dernière modification de la notice
03/03/2018 15:49
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