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C-terminal amino acid sequences of two phytochromes sharing less than 40 per cent homol­ogy and two transmitter modules of bacterial sensor proteins that share homologies with phy­tochromes were examined by hydrophobic cluster analysis. Striking coincidences in distribu­tion, size, shape and orientation of hydrophobic and hydrophilic domains of the bacterial transmitter modules and phytochrome sequences were revealed. The results corroborate the view that the folding of the homologous regions of the two groups of proteins is similar. Since the mode of action of phytochrome is not known, the structural coincidences may be indica­tive of how phytochrome transmits signals, although distinct differences should not be over­ looked. Some coinciding structural features in phytochromes and bacterial sensors may tenta­tively be extracted from secondary structure predictions.

zeitschrift für naturforschung c

Are Bacterial Sensory Systems Models for Phytochrome Action? Hydrophobic Cluster Analysis of the Phytochrome Module Related to Bacterial Transmitter Modules