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pubmed:abstractText |
NF-Y is a CCAAT box binding protein critical for the expression of diverse eukaryotic genes. We have purified the A and B subunits of NF-Y and, using microsequencing and PCR technology, have cloned the corresponding cDNAs. NF-YA and NF-YB show stretches of arresting sequence homology to the yeast transcriptional activators HAP2 and HAP3. Unlike their yeast counterparts, however, the two mouse subunits appear necessary and sufficient for CCAAT binding activity. We hypothesize that in the case of NF-Y, DNA binding and dimerization both rely on residues within the homology domains, which include rather suggestive 'half-finger' motifs.
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