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First published online March 9, 2004
Journal of Experimental Biology 207, 1323-1334 (2004)
Published by The Company of Biologists 2004
doi: 10.1242/jeb.00898

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Structure–function analysis of the cysteine string protein in Drosophila: cysteine string, linker and C terminus

Christine Arnold^1,*, Natascha Reisch^1,*, Christian Leibold^1,*, Sonja Becker¹, Kristina Prüfert¹, Kerstin Sautter¹, Dieter Palm², Susanne Jatzke¹, Sigrid Buchner¹ and Erich Buchner^1,

¹ Lehrstuhl für Genetik und Neurobiologie, Theodor-Boveri-Institut für Biowissenschaften, Am Hubland, D-97074 Würzburg, Germany
² Lehrstuhl für Physiologische Chemie I, Theodor-Boveri-Institut für Biowissenschaften, Am Hubland, D-97074 Würzburg, Germany

Author for correspondence (e-mail: buchner{at}biozentrum.uni-wuerzburg.de)

Accepted 26 January 2004

Cysteine string proteins (CSPs) are conserved secretory vesicle proteins involved in regulating neurotransmitter and peptide release. While the function of the J-domain has been studied in detail, little is known about other conserved regions. We have constructed mutant genes coding for proteins with modified cysteine string, linker region or C terminus and transformed them into Csp null-mutant Drosophila. In the living animal, mutated CSP lacking all cysteines fails to associate with membranes, does not concentrate in synaptic terminals, and cannot rescue adult temperature-sensitive paralysis and short life span, both prominent null mutant phenotypes. A mutant protein with 5 instead of 11 string cysteines appears to be normally targeted but cannot rescue paralysis at 37°C. We propose that the cysteine string, in addition to its role in targeting, may be essential for a function of CSP that is dependent on the number of cysteines in the string. A deletion in the linker region or the C terminus does not affect CSP targeting, and function in adults is only marginally impaired.

Key words: cysteine string protein (CSP), secretory vesicle, Drosophila, in vitro mutagenesis, protein targeting, paralysis, life span

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