High impact information on SUC1

• Among the proton-sucrose symporters cloned to date, only the histidine residue at position 65 of AtSUC1 from Arabidopsis thaliana is conserved across species [1].
• This paper describes the sites of AtSUC1 gene expression and AtSUC1 protein localization and assigns specific functions to this sucrose transporter in anther development and pollen tube growth [2].
• The AtSUC1 sucrose carrier may represent the osmotic driving force for anther dehiscence and pollen tube growth in Arabidopsis [2].
• The Arabidopsis AtSUC1 protein has previously been characterized as a plasma membrane H+-sucrose symporter [2].
• In situ hybridizations identified AtSUC1 expression in anther connective tissue, in funiculi and in fully developed pollen grains [2].

Biological context of SUC1

• The SUC1/CKS1 proteins interact with cyclin-dependent kinases (CDKs) and play an essential, but yet not entirely resolved, role in the regulation of the cell cycle [3].

Anatomical context of SUC1

• This paper describes functional expression in Saccharomyces cerevisiae of two cDNAs encoding energy-dependent sucrose transporters from the plasma membrane of Arabidopsis thaliana, SUC1 and SUC2 [4].
• A kinetic model with ordered cytoplasmic dissociation for SUC1, an Arabidopsis H+/sucrose cotransporter expressed in Xenopus oocytes [5].

Associations of SUC1 with chemical compounds

• SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana; expression and characterization in baker's yeast and identification of the histidine-tagged protein [4].
• A modified SUC1-His6 cDNA encoding a histidine tag at the SUC1 C-terminus was also expressed in S. cerevisiae [4].
• This increase in fixation and export was supported by increased expression of the plastidic triose-phosphate transporter AtTPT and, to a lesser extent, the high-affinity Suc transporter AtSUC1 [6].
• AtSUC1 is also expressed in roots and external application of sucrose increased AtSUC1 expression in roots [7].

Other interactions of SUC1

• The two proteins exhibit different patterns of pH dependence with SUC1 being much more active at neutral and slightly acidic pH values than SUC2 [4].

Analytical, diagnostic and therapeutic context of SUC1

• ELISA assays run with microsomal fractions and PMV using the AtSUC1 sucrose transporter probe indicated that ageing, and to a lesser extent cutting, increased the amount of sucrose transporter present in the plasma membrane [8].

References