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HOMOLOGY AT THE AMINO ACID LEVEL BETWEEN PLANT PHYTOCHROMES AND A REGULATOR OF ASEXUAL SPORULATION IN Emericella (=Aspergillus) nidulans
Author(s) -
Grifith Gareth W.,
Jenkins Gareth I.,
MilnerWhite E. James,
Clutterbuck A. John
Publication year - 1994
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1994.tb05030.x
Subject(s) - aspergillus nidulans , phytochrome , biology , mutant , structural similarity , botany , biochemistry , gene , red light
–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.