The storage glutelin in rice ( Oryza sativa L.) seeds could be separated at least into more than 13 acidic and 19 basic polypeptides by two dimensional electrophoresis. Rice glutelin might be mainly controlled by abou...The storage glutelin in rice ( Oryza sativa L.) seeds could be separated at least into more than 13 acidic and 19 basic polypeptides by two dimensional electrophoresis. Rice glutelin might be mainly controlled by about six major genes according to the expression of glutelin polypeptides. The acidic polypeptide of glutelin could be clearly separated into two groups by peptide mapping and N-terminal amino acid sequence analysis. These two groups were just in accord with the GluA and GluB subfamilies exactly.展开更多
Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amp...Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amplification of cDNA Ends(RACE) technique, full-length cDNA and DNA sequences of ghrelin gene were obtained. The full-length ghrelin cDNA(GenBank accession no. JX122807) was 552 bp long, containing a 115 bp 5'-untranslated region, a 324 bp open reading frame and a 113 bp 3'-untranslated region. The full-length ghrelin DNA was 1 323 bp, consisting of three introns and four exons. The exon/intron junction sequences conformed to the GT/AG rule. Three introns were 594, 84 and 93 bp in length, respectively; four exons were229, 78, 112 and 133 bp in length, respectively. The results of amino acid sequence analysis showed that the deduced propreghrelin sequence of M. albus contained a signal peptide(SP) consisting of 22 amino acid residues, a mature peptide(MP)consisting of 19 amino acid residues and a C-terminal amino acid residue. Among them, the third amino acid of MP was serine(Ser^3) as the site for N-acylation and N-deacetylation reactions; the C-terminal amino acid residue sequence might contain a peptide hormone obestatin, which is a physiological antagonist of mature Ghrelin peptide. The homology and phylogenic relationships analyses of amino acid sequences suggested that propreghrelin of M. albus had high similarity to those of several Perciformes fishes; the propreghrelins of M. albus, Perciformes and Heterosomata fishes were clustered into a subgroup. The high conservatism of the gene structure and the amino acid sequences indicated that Ghrelin exerts important physiological functions and plays similar physiological mechanisms in vertebrates.展开更多
文摘The storage glutelin in rice ( Oryza sativa L.) seeds could be separated at least into more than 13 acidic and 19 basic polypeptides by two dimensional electrophoresis. Rice glutelin might be mainly controlled by about six major genes according to the expression of glutelin polypeptides. The acidic polypeptide of glutelin could be clearly separated into two groups by peptide mapping and N-terminal amino acid sequence analysis. These two groups were just in accord with the GluA and GluB subfamilies exactly.
基金Supported by Natural Science Foundation of Hubei Province(2013CFB393)Open Fund of Key Laboratory of Freshwater Fisheries and Germplasm Resources Utilizations,Ministry of Agriculture(KF201307)+2 种基金National Pillar Program of China(2013BAD20B06)Pillar Program of Hubei Province(2015BBA235)Program for Outstanding Young and Middle-aged Scientific Innovation Team in Colleges and Universities of Hubei Province(T201503)
文摘Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amplification of cDNA Ends(RACE) technique, full-length cDNA and DNA sequences of ghrelin gene were obtained. The full-length ghrelin cDNA(GenBank accession no. JX122807) was 552 bp long, containing a 115 bp 5'-untranslated region, a 324 bp open reading frame and a 113 bp 3'-untranslated region. The full-length ghrelin DNA was 1 323 bp, consisting of three introns and four exons. The exon/intron junction sequences conformed to the GT/AG rule. Three introns were 594, 84 and 93 bp in length, respectively; four exons were229, 78, 112 and 133 bp in length, respectively. The results of amino acid sequence analysis showed that the deduced propreghrelin sequence of M. albus contained a signal peptide(SP) consisting of 22 amino acid residues, a mature peptide(MP)consisting of 19 amino acid residues and a C-terminal amino acid residue. Among them, the third amino acid of MP was serine(Ser^3) as the site for N-acylation and N-deacetylation reactions; the C-terminal amino acid residue sequence might contain a peptide hormone obestatin, which is a physiological antagonist of mature Ghrelin peptide. The homology and phylogenic relationships analyses of amino acid sequences suggested that propreghrelin of M. albus had high similarity to those of several Perciformes fishes; the propreghrelins of M. albus, Perciformes and Heterosomata fishes were clustered into a subgroup. The high conservatism of the gene structure and the amino acid sequences indicated that Ghrelin exerts important physiological functions and plays similar physiological mechanisms in vertebrates.
