Cloning and expression analysis of carboxyl-terminal protease cDNA from Gossypium hirsutum L.
A full-length cotton cDNA,designated GhCtp, was isolated from Gossypium hirsutum L. by the PCR-based cDNA library screening. The cDNA encodes a polypeptide of 473-amino acid residues. Sequence alignment showed that GhCtp was highly homologous to a family of carboxyl-terminal proteases (Ctp) from other species. GhCtp is a potential transmembrane protease, and comprises a conserved domain numbered DUF239 at its carboxyl-terminal and an arginine-rich region at the amino-terminal, respectively. Furthermore, there is a putative ATP-/GTP-binding site motif A (P-loop) in GhCtp which do not exist in Ctps of Arabidopsis and Oryza, indicating that GhCtp might function in a manner different from other Ctps. RT-PCR analysis suggested that GhCtp was not a fiber-specific or -preferential gene, and had a low expression level in different tissues or developmental stages of cotton.
Jiang
Jian-Xiong
JX
National Key Laboratory of Crop Genetics and Germplasm Enhancement, Cotton Research Institute, Nanjing Agricultural University, Nanjing 210095, China. jxjiang2002@yahoo.com.cn
Zhang
Tian-Zhen
TZ
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000302:isolation & purification; D010450:Endopeptidases / Q000737:chemistry / Q000235:genetics*; D003368:Gossypium / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data
D018076:DNA, Complementary; D010450:Endopeptidases