Distribution and functional analysis of the two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria
In the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two isozymes of 8-vinyl reductase have been described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB . Only BciB contains an [Fe-S...
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Published in: | Archives of microbiology Vol. 203; no. 6; pp. 3565 - 3575 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
Berlin/Heidelberg
Springer Berlin Heidelberg
01-08-2021
Springer Nature B.V |
Subjects: | |
Online Access: | Get full text |
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Summary: | In the chlorophyll biosynthesis pathway, the 8-vinyl group of the chlorophyll precursor is reduced to an ethyl group by 8-vinyl reductase. Two isozymes of 8-vinyl reductase have been described in oxygenic photosynthetic organisms: one encoded by
BciA
and another by
BciB
. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form; whereas a few contain
BciA
. Given this disparity in distribution, cyanobacterial BciA has remained largely overlooked, which has limited understanding of chlorophyll biosynthesis in these microorganisms. Here, we reveal that cyanobacterial
BciA
encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant
Synechococcus
and
Acaryochloris
BciA. Genomic comparison revealed that
BciB
had been replaced by
BciA
during evolution of the marine cyanobacterium
Synechococcus
, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of
BciA
confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0302-8933 1432-072X |
DOI: | 10.1007/s00203-021-02348-w |