Y. Nishii et al., CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated from cisplatin-resistant cell line, FEBS LETTER, 465(2-3), 2000, pp. 153-156
A novel putative SR protein, designated cisplatin resistance-associated ove
rexpressed protein (CROP), has been cloned from cisplatin-resistant cell li
nes by differential display. The N-half of the deduced amino acid sequence
of 432 amino acids of CROP contains cysteine/histidine motifs and leucine z
ipper-like repeats. The C-half consists mostly of charged and polar amino a
cids: arginine (58 residues or 25%), glutamate (36 residues or 16%), serine
(35 residues or 15%), lysine (30 residues, 13%), and aspartate (20 residue
s or 9%), The C-half is extremely hydrophilic and comprises domains rich in
lysine and glutamate residues, rich in alternating arginine and glutamate
residues, and rich in arginine and serine residues. The arginine/serine-ric
h domain is dominated by a series of 8 amino acid imperfect repetitive moti
f (consensus sequence, Ser-Arg-Ser-Arg-Asp/Glu-Arg-Arg-Arg), which has been
found in RNA splicing factors. The RNase protection assay and Western blot
ting analysis indicate that the expression of CROP is about 2-3-fold higher
in mRNA and protein levels in cisplatin-resistant ACHN/CDDP cells than in
host ACHN cells. CROP is the human homologue of yeast Luc7p, which is suppo
sed to be involved in 5'-splice site recognition and is essential for veget
ative growth. (C) 2000 Federation of European Biochemical Societies.