High impact information on NIT2

• The GLN3 protein contains a single putative Cys2/Cys2 zinc finger which has homology to the Neurospora crassa NIT2 protein, the Aspergillus nidulans AREA protein, and the erythroid-specific transcription factor GATA-1 [1].
• One of these alpha-helical regions occurs within the zinc finger DNA-binding domain of NIT2 [2].
• NIT2 binds to upstream activation sites which contain at least two GATA core elements in the promoter regions of the nitrogen-controlled structural genes, and activates their transcription, possibly by way of acidic activation domains [2].
• Interestingly, and also in contrast to the HIS4 regulation in S. cerevisiae, we found domains for Nit2-like and yeast-Ap1-like binding sequences [3].
• Several GCN4- and NIT2-binding motifs have been matched in the promotor sequence of PsLYS2 [4].

Biological context of NIT2

• Four high-affinity binding sites for the NIT2 protein were found within a central region of the nit-2 gene itself [5].

Associations of NIT2 with chemical compounds

• Expression of nit-3 and nit-6, the structural genes which encode nitrate reductase and nitrite reductase in Neurospora crassa, requires the global-acting NIT2 and the pathway specific NIT4 regulatory proteins [6].

Physical interactions of NIT2

• NIT2 binding sites in the promoter regions of nit3, alc and lao have at least two GATA sequence elements [5].

Other interactions of NIT2

• We have examined the binding affinity of the NIT2 protein for the yeast DAL5 wild-type upstream activation sequence UASNTR, which contains two GATA elements, and for a series of mutated binding sites, each differing from the wild-type site by a single base [5].

References