Nuclear factor I (NFI) proteins constitute a large family of eukaryoti
c DNA binding proteins. They are involved in viral and cellular aspect
s of transcriptional regulation and they are capable of stimulating ad
enovirus initiation of replication. Using in vitro translated NFI prot
eins encoded by four different chicken NFI genes, we have detected hom
odimers as well as heterodimers for all combinations tested. The forma
tion of heterodimers was critically dependent on cotranslation, indica
ting stable dimer formation in the absence of DNA. The unrestricted he
terodimerization of NFI proteins adds, beside gene diversity and alter
native splicing, another level of diversity to this protein family.