Homology at the amino acid level between plant phytochromes and a regulator of asexual sporulation in Emericella (= Aspergillus) nidulans.
Protein sequence comparison between the N-terminal regions of the BRLA (bristle A) protein of the ascomycete fungus Aspergillus nidulans and a number of plant phytochromes has demonstrated a moderate level of sequence similarity. The region of similarity corresponds to the phytochrome domains believed to be responsible for photoreception and which undergo light-induced conformational changes, although a putative chromophore-binding site is not evident. Over 22% of residues are conserved and 24% conservatively substituted between residues 1 and 272 of BRLA and the N-terminal domains of Type 1 phytochromes from dicotyledonous species. A lower level of similarity, but over the same region, is observed in comparison with a wider range of phytochromes. Given the known role of BRLA as a transcriptional activator involved in conidiation, and the red/far-red reversible photoregulation of this developmental process, the similarity with phytochromes may be significant.
Griffith
G W
GW
Department of Genetics, University of Glasgow, Scotland, UK.
Jenkins
G I
GI
Milner-White
E J
EJ
Clutterbuck
A J
AJ
D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000235:genetics / Q000528:radiation effects; D005656:Fungal Proteins / Q000235:genetics*; D008027:Light; D008969:Molecular Sequence Data; D010834:Phytochrome / Q000235:genetics*; D010944:Plants / Q000235:genetics / Q000528:radiation effects; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors
C063497:BRLA protein, Emericella nidulans; D005656:Fungal Proteins; D014157:Transcription Factors; D010834:Phytochrome