A putative lplant homolog of the yeast P - l , 3 - glucan synthase subunit FKSI from ' cotton ( Gossypium hirsutum L . ) fibers
نویسندگان
چکیده
A novel plant gene CFLl was cloned from cotton (GossJPium hirsutum L.) fibers by expressed se quence tag (EST) database searching and 5'-RACE (rapid amplification of eDNA ends). This gene shows sequence homology with FKSl which has been identified as the putative catalytic subunit of the yeast fi-1,3-glucan syn thase. It encodes a protein (CFLlp) of 219 kDa with 13 deduced transmembrane helices and 2 large hydrophilic domains, one of which is at the N-terminus and the other in the intcrnal region of the polypeptide. CFLl displays 21 % identity and 41 % similarity to FKSl at the amino acid level over its entire length, with 31 % identi ty and 52% similarity for the hydrophilic central domain. Using RNA and protein blot analysis, CFLl was found to be expressed at higher levels in cotton fibers during primary wall development. CFLl also had a strong expression in young roots. Using a calmodulin (CaM)-gel overlay assay, the hydrophilic N-terminal domain of CFLI p was shown to bind to CaM, while the hydrophilic central domain did not. A putative CaM-binding domain, 16 amino acids long, was predicted in the hydrophilic N terminal domain. Moreover, a product-entrapment assay demonstrated that a protcin associated with an in vitro synthesized callose pellet could be labclcd by anti-CFLl antibodies. Our finding suggests that CFLl is a putative plant homolog of the yeast fi-I J-glucan synthase su bunit FKSl and could be involved in callose synthesis
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