Had. Johard et al., The highly conserved synapse protein SNAP-25 displays sequence variabilityin the cockroach Leucophaea maderae, COMP BIOC B, 122(1), 1999, pp. 63-68
Citations number
25
Categorie Soggetti
Biochemistry & Biophysics
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
SNAP-25 (synaptosome-associated protein of 25 kD) is attached to the intrac
ellular side of presynaptic membranes where it serves as a target receptor
for the vesicle docking machinery prior to release of neurotransmitter. SNA
P-25 displays a high degree of sequence conservation between vertebrates an
d Drosophila melanogaster. To obtain more information about conserved regio
ns of SNAP-25, we have isolated cDNA clones from the cockroach Leucophaea m
aderae. One clone (Lm1) encoded a full-length SNAP-25 protein and its deduc
ed amino acid sequence is 77% identical to Drosophila SNAP-25. Surprisingly
, the cockroach protein is 17 amino acids shorter than Drosophila SNAP-25 a
t the carboxy terminus. Four other cDNA clones encode parts of SNAP-25 and
each clone has distinct characteristics, including amino acid replacements
and unique carboxy termini. Thus, the highly conserved protein SNAP-25 disp
lays unexpected sequence variability in the cockroach that may indicate spe
cialized SNAP-25 isoforms. (C) 1999 Elsevier Science Inc. All rights reserv
ed.