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Function of sequence insertions in the myosin IX motor domain

Reference	C16025
Principal Investigator / Supervisor	Professor Michelle Peckham
Co-Investigators / Co-Supervisors	Professor Peter Knight
Institution	University of Leeds
Department	Human Biology
Funding type	Research
Value (£)	75,096
Status	Completed
Type	Research Grant
Start date	13/02/2002
End date	12/08/2003
Duration	18 months

Abstract

The motor domain of all known myosins contains a conserved sequence core for binding to actin and hydrolysing ATP. This core is embedded within highly variable sequences that are presumed to adapt the motor to a wide range of specific cellular roles. This presumption has scarcely been tested. The motor domain of myosin IX is notable for two large insertions of unknown significance. To determine their function, we will use high resolution electron microscopy to compare the structures of wild type myosin IX attached to actin with mutants that lack these inserts, both with and without ATP. We will correlate these data with the activity of the mutants assessed by enzyme kinetics, motility assays and location and function in living cells.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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