A model for Batten disease protein CLN3: functional implications from homology and mutations.
In an attempt to understand the molecular nature of Batten disease, we have examined the amino acid sequence of the affected CLN3 gene product (The International Batten Disease Consortium (1995) Cell 82, 949-957) and the site-specific mutations which give rise to the biological defect. Homology searches and molecular modeling have led to the development of a model for the folding and disposition of the protein, possibly within a mitochondrial membrane. High homology with a yeast protein of unknown function suggests a strong evolutionary conservation of function. We speculate that a possible role for the protein may be in chaperoning the folding/unfolding or assembly/ disassembly of other proteins, specifically subunit c of the mitochondrial ATP synthase complex.
Janes
R W
RW
Department of Crystallography, Birkbeck College, University of London, UK.
Munroe
P B
PB
Mitchison
H M
HM
Gardiner
R M
RM
Mole
S E
SE
Wallace
B A
BA
D000595:Amino Acid Sequence; D016213:Cyclins; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics*; D018832:Molecular Chaperones / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D009472:Neuronal Ceroid-Lipofuscinoses / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid
C079895:CLN3 protein, S cerevisiae; C105199:CLN3 protein, human; D016213:Cyclins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins