: The present study is aimed to investigate the mechanism of the biochemical genetic in short-seasoned cotton (Gossypium hirsutum L.) (SSC). Ten cultivars from two types of SSC were selected, five SSC with no prematur...: The present study is aimed to investigate the mechanism of the biochemical genetic in short-seasoned cotton (Gossypium hirsutum L.) (SSC). Ten cultivars from two types of SSC were selected, five SSC with no premature senescence crossed with five SSC with premature senescence. The parents, F1, and F2 from the reciprocal crosses were field tested in replication in 2001 and 2002. The results indicated that the activities of protective enzymes of the antioxidant system, such as catalase (CAT), superoxide dismutase (SOD), and peroxidase (POD), were higher in the early maturing SSC with premature senescence compared with activities in the SSC parental cultivars that showed premature senescence, whereas the malondialdehyde (MD A) content in former group was lower than that in latter group. Various genetic variances and heritabilities for these biochemical traits and auxin (IAA), abscisic acid (ABA), and chlorophyll (Chl a+b) contents were also estimated. Significant additive variance for CAT, POD, ABA, and IAA existed, whereas CAT specific activity and SOD activity were largely controlled by dominant effects. Both maternal and dominant variances played equally predominant roles in the specific activity of POD and SOD, MDA, and soluble portents. The relative contribution of the various genetic components to the phenotypic variation varied in the boll-setting period.展开更多
A gene encoding a cysteine proteinase was iso- lated from senescent leave of cotton (Gossypium hirsutum) cv liaomian No. 9 by utilizing rapid amplification of cDNA ends polymerase chain reaction (RACE-PCR), and a set ...A gene encoding a cysteine proteinase was iso- lated from senescent leave of cotton (Gossypium hirsutum) cv liaomian No. 9 by utilizing rapid amplification of cDNA ends polymerase chain reaction (RACE-PCR), and a set of con- sensus oligonucleotide primers was designed to anneal the conserved sequences of plant cysteine protease genes. The cDNA, which designated Ghcysp gene, contained 1368 bp terminating in a poly(A)+ trail, and included a putative 5 (98 bp) and a 3 (235 bp) non-coding region. The opening reading frame (ORF) encodes polypeptide 344 amino acids with the predicted molecular mass of 37.88 kD and theoretical pI of 4.80. A comparison of the deduced amino acid sequence with the sequence in the GenBank database has shown consider- able sequence similarity to a novel family of plant cysteine proteases. This putative cotton Ghcysp protein shows from 67% to 82% identity to the other plants. All of them share catalytic triad of residues, which are highly conserved in three regions. Hydropaths analysis of the amino acid se- quence shows that the Ghcysp is a potential membrane pro- tein and localizes to the vacuole, which has a transmembrane helix between resides 7 —25. A characteristic feature of Ghcysp is the presence of a putative vacuole-targeting signal peptide of 19-amino acid residues at the N-terminal region. The expression of Ghcysp gene was determined using north- ern blot analysis. The Ghcysp mRNA levels are high in de- velopment senescent leaf but below the limit of detection in senescent root, hypocotyl, faded flower, 6 d post anthesis ovule, and young leaf.展开更多
文摘: The present study is aimed to investigate the mechanism of the biochemical genetic in short-seasoned cotton (Gossypium hirsutum L.) (SSC). Ten cultivars from two types of SSC were selected, five SSC with no premature senescence crossed with five SSC with premature senescence. The parents, F1, and F2 from the reciprocal crosses were field tested in replication in 2001 and 2002. The results indicated that the activities of protective enzymes of the antioxidant system, such as catalase (CAT), superoxide dismutase (SOD), and peroxidase (POD), were higher in the early maturing SSC with premature senescence compared with activities in the SSC parental cultivars that showed premature senescence, whereas the malondialdehyde (MD A) content in former group was lower than that in latter group. Various genetic variances and heritabilities for these biochemical traits and auxin (IAA), abscisic acid (ABA), and chlorophyll (Chl a+b) contents were also estimated. Significant additive variance for CAT, POD, ABA, and IAA existed, whereas CAT specific activity and SOD activity were largely controlled by dominant effects. Both maternal and dominant variances played equally predominant roles in the specific activity of POD and SOD, MDA, and soluble portents. The relative contribution of the various genetic components to the phenotypic variation varied in the boll-setting period.
文摘A gene encoding a cysteine proteinase was iso- lated from senescent leave of cotton (Gossypium hirsutum) cv liaomian No. 9 by utilizing rapid amplification of cDNA ends polymerase chain reaction (RACE-PCR), and a set of con- sensus oligonucleotide primers was designed to anneal the conserved sequences of plant cysteine protease genes. The cDNA, which designated Ghcysp gene, contained 1368 bp terminating in a poly(A)+ trail, and included a putative 5 (98 bp) and a 3 (235 bp) non-coding region. The opening reading frame (ORF) encodes polypeptide 344 amino acids with the predicted molecular mass of 37.88 kD and theoretical pI of 4.80. A comparison of the deduced amino acid sequence with the sequence in the GenBank database has shown consider- able sequence similarity to a novel family of plant cysteine proteases. This putative cotton Ghcysp protein shows from 67% to 82% identity to the other plants. All of them share catalytic triad of residues, which are highly conserved in three regions. Hydropaths analysis of the amino acid se- quence shows that the Ghcysp is a potential membrane pro- tein and localizes to the vacuole, which has a transmembrane helix between resides 7 —25. A characteristic feature of Ghcysp is the presence of a putative vacuole-targeting signal peptide of 19-amino acid residues at the N-terminal region. The expression of Ghcysp gene was determined using north- ern blot analysis. The Ghcysp mRNA levels are high in de- velopment senescent leaf but below the limit of detection in senescent root, hypocotyl, faded flower, 6 d post anthesis ovule, and young leaf.
