Cloning Shrunken 2 (Sh2) gene from h14 maize cultivar and constructing transformation vector pcambia 1301-Ubi-Sh2
نویسندگان
چکیده
منابع مشابه
The SH2 domain interaction landscape.
Members of the SH2 domain family modulate signal transduction by binding to short peptides containing phosphorylated tyrosines. Each domain displays a distinct preference for the sequence context of the phosphorylated residue. We have developed a high-density peptide chip technology that allows for probing of the affinity of most SH2 domains for a large fraction of the entire complement of tyro...
متن کاملIdentification and molecular characterization of shrunken-2 cDNA clones of maize.
Mutation at the shrunken-2 (Sh2) locus of maize, a gene described more than 40 years ago, greatly reduces starch levels in the endosperm through its effect on the starch synthetic enzyme ADP-glucose pyrophosphorylase, an enzyme thought to be regulatory in this biosynthetic pathway. Although our previous work has suggested that Sh2 is a structural gene for this enzyme, we have also reported data...
متن کاملStructure and function of SH2 domains.
In order for cells to respond to their environment, a series of regulated molecular events has to take place. External signalling molecules bind to cellular receptors and thereby trigger the activation of multiple intracellular pathways, which modify cellular phenotypes. The cell-surface receptors for a wide range of polypeptide hormones possess protein tyrosine kinase activity, which is induce...
متن کاملStructure and specificity of the SH2 domain
In 1992 and 1993, we published two papers that described the structure of the Src homology 2 (SH2) domain of the v-Src tyrosine kinase complexed to nonspecific phosphotyrosyl peptides (Waksman et al., 1992) and to a phosphopeptide that has specificity for the Src SH2 domain (Waksman et al., 1993). These papers mark the beginnings of a research effort on the Src kinases that has resulted ten yea...
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ژورنال
عنوان ژورنال: TAP CHI SINH HOC
سال: 2014
ISSN: 0866-7160,0866-7160
DOI: 10.15625/0866-7160/v35n3se.3849