Multiple defects in the activity of adenylate cyclase from the Drosophila memory mutant rutabaga.

Abstract:

:Adenylate cyclase in homogenates of Drosophila melanogaster is heterogeneous with respect to its affinity toward MgATP and its subcellular distribution. Km values for MgATP range, under similar assay conditions, from approximately 10(-5) M to approximately 10(-3) M, depending on the body region and on the subcellular localization of the enzyme. The majority of the enzyme in whole-body preparations is particulate, but various body regions differ in the relative proportion of the soluble enzyme. The memory mutant rutabaga lacks up to 35% of the total particulate activity. Even ligands that stimulate directly the catalytic subunit are incapable of bringing the activity of the mutant's enzyme to normal levels. The defect is differentially pronounced in various body parts and is associated with an altered responsiveness of the enzyme to Mg2+, to Ca2+, and to forskolin. It is suggested that rutabaga is lesioned in a subpopulation, or a functional state, of adenylate cyclase, which may play a role in memory formation.

journal_name

J Neurochem

authors

Dudai Y,Zvi S

doi

10.1111/j.1471-4159.1985.tb03996.x

subject

Has Abstract

pub_date

1985-08-01 00:00:00

pages

355-64

issue

2

eissn

0022-3042

issn

1471-4159

journal_volume

45

pub_type

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