Resolving the fungal velvet domain architecture by <i>Aspergillus nidulans</i> VelB.

ABSTRACT: Velvet transcription factors are found throughout the fungal kingdom and share a common velvet domain with a fold similar to that of animal NF-κB. They act as homodimeric or heterodimeric master regulators of fungal secondary metabolism, development, and differentiation. A comparison of velvet domains from 4,999 fungal velvet proteins revealed a conserved overall architecture, including an N-terminal DNA-binding region of approximately 30 amino acids and a C-terminal dimerization region of about 100 amino acids. The dimerization region comprises α- and β-subunits separated by a linker region. A detailed analysis of the velvet domain in Aspergillus nidulans VelB identified glycine (glycine 240) and leucine (leucine 331) residues in the dimerization region as critical for interactions

SUBMITTER: Chen W 

PROVIDER: S-EPMC12077163 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature