Disease relevance of AT1G16280

• The results of phage display screen using recombinant protein, confirmed by direct yeast two-hybrid analyses, indicate that AtSWI3B interacts with FCA, a regulator of flowering time in ARABIDOPSIS: This interaction is through the C-terminal region of FCA, located outside the conserved RNA- and protein-binding domains of this protein [1].

High impact information on AT1G16280

• Autoregulation of FCA pre-mRNA processing controls Arabidopsis flowering time [2].
• We demonstrate here that FCA negatively regulates its own expression by ultimately promoting cleavage and polyadenylation within intron 3 [2].
• The phenotypes of the 3' end formation esp mutants include impaired termination of the transgene transcripts, early flowering, and enhanced silencing of the FCA-beta mRNA [3].
• One of them, the FCA gene, turns out to encode an RNA binding protein [4].
• Novel slicing isoforms were generated from FCA pre-mRNA by splicing of noncanonical introns in plants with altered expression levels of atU2AF35 [5].

Biological context of AT1G16280

• We show that this negative autoregulation is under developmental control and requires the FCA WW protein interaction domain [2].
• In order to acquire further insight into the control of heading dates in rice, we isolated and conducted an expression analysis on OsFCA, which exhibited 38% sequence homology with Arabidopsis FCA [6].
• The overexpression of OsFCA cDNA, driven by the 35S promoter, was shown to partially rescue the late flowering phenotype of the fca mutant, suggesting that the functions of the OsFCA and the FCA are partially overlapped, despite the lack of an apparent FLC homologue in the rice genome [6].
• Overexpression of AGL28 caused precocious flowering via the upregulation of the expression of FCA and LUMINIDEPENDENS (LD), both floral promoters within the autonomous pathway [7].
• We report here its demonstration in a plant genome by reconstructing the physical map of a 1.9 Mbp region around the FCA locus of Arabidopsis thaliana [8].

Associations of AT1G16280 with chemical compounds

• The N-terminal region of the OsFCA protein appears to be unusually rich in glycine-residues, unlike the N-terminal region found in FCA [6].

Analytical, diagnostic and therapeutic context of AT1G16280

• The fluorescence quantitative PCR analysis showed that the mRNA of OsFCA-1 is the most abundant in the four splicing variants of rice FCA, and its expression level is much higher in differentiating calli than in calli [9].

References