Drosophila actin mutants and the study of myofibrillar assembly and function.
The use of Drosophila mutations in the indirect flight muscle-specific actin gene, Act88F, to study actin structure/function and its assembly into thin filaments during myofibrillogenesis is described. Mutants with different phenotypic effects are discussed and attempts made to correlate the different properties of the mutants in vivo-myofibrillar structure, actin synthesis, accumulation and stability, heat shock response induction-with properties of the same mutations expressed by in vitro transcription/translation of the cloned actin genes-co-polymerisation, thermostability and protein conformation. Few of the properties show a complete correlation between the different classes of mutants. The nature of the diversity of the mutant effects is discussed. Questions as to how this will help in elucidating the molecular effects of the mutations and the assembly of thin filaments and myofibrils are considered. In addition, the efficacy of the co-polymerisation assay is examined. The post-translational processing of this actin-by N-terminal processing, methylation and ubiquitination-are described. Data is presented that inhibition of the N-terminal processing of actin in vitro affects the ability of the actin to copolymerise, and makes unprocessed actin behave as a capping protein. The possible in vivo importance of this phenomenon is discussed.
Sparrow
J C
JC
Department of Biology, University of York, U.K.
Drummond
D R
DR
Hennessey
E S
ES
Clayton
J D
JD
Lindegaard
F B
FB
D000199:Actins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D004330:Drosophila / Q000235:genetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009132:Muscles / Q000737:chemistry* / Q000648:ultrastructure; D009154:Mutation; D011499:Protein Processing, Post-Translational / Q000502:physiology; D013329:Structure-Activity Relationship
D000199:Actins; D046911:Macromolecular Substances