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Title: Evolutionary Significance of an Algal Gene Encoding an [FeFe]-Hydrogenase with F-Domain Homology and Hydrogenase Activity in Chlorella Variabilis NC64A

Abstract

[FeFe]-hydrogenases (HYDA) link the production of molecular H{sub 2} to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H{sub 2}-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogsmore » are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases.« less

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE Office of Science, Basic Energy Sciences and Joint Genome Institute; US Air Force Office of Scientific Research (AFOSR); National Aeronautic and Space Administration (NASA)
OSTI Identifier:
1036398
DOE Contract Number:  
AC36-08GO28308
Resource Type:
Journal Article
Journal Name:
Planta
Additional Journal Information:
Journal Volume: 234; Journal Issue: 4; Journal ID: ISSN 0032-0935
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 54 ENVIRONMENTAL SCIENCES; ALGAE; ANOXIA; BACTERIA; CHLAMYDOMONAS; CHLORELLA; DIATOMS; ELECTRONS; ENZYMES; FERMENTATION; GENES; HYDROGENASES; IN VIVO; METABOLISM; ORIGIN; PRODUCTION; SPLICING; TRANSPORT; Chemical and Biosciences

Citation Formats

Meuser, J. E., Boyd, E. S., Ananyev, G., Karns, D., Radakovits, R., Murthy, U. M. N., Ghirardi, M. L., Dismukes, G. C., Peters, J. W., and Posewitz, M. C. Evolutionary Significance of an Algal Gene Encoding an [FeFe]-Hydrogenase with F-Domain Homology and Hydrogenase Activity in Chlorella Variabilis NC64A. United States: N. p., 2011. Web. doi:10.1007/s00425-011-1431-y.
Meuser, J. E., Boyd, E. S., Ananyev, G., Karns, D., Radakovits, R., Murthy, U. M. N., Ghirardi, M. L., Dismukes, G. C., Peters, J. W., & Posewitz, M. C. Evolutionary Significance of an Algal Gene Encoding an [FeFe]-Hydrogenase with F-Domain Homology and Hydrogenase Activity in Chlorella Variabilis NC64A. United States. doi:10.1007/s00425-011-1431-y.
Meuser, J. E., Boyd, E. S., Ananyev, G., Karns, D., Radakovits, R., Murthy, U. M. N., Ghirardi, M. L., Dismukes, G. C., Peters, J. W., and Posewitz, M. C. Sat . "Evolutionary Significance of an Algal Gene Encoding an [FeFe]-Hydrogenase with F-Domain Homology and Hydrogenase Activity in Chlorella Variabilis NC64A". United States. doi:10.1007/s00425-011-1431-y.
@article{osti_1036398,
title = {Evolutionary Significance of an Algal Gene Encoding an [FeFe]-Hydrogenase with F-Domain Homology and Hydrogenase Activity in Chlorella Variabilis NC64A},
author = {Meuser, J. E. and Boyd, E. S. and Ananyev, G. and Karns, D. and Radakovits, R. and Murthy, U. M. N. and Ghirardi, M. L. and Dismukes, G. C. and Peters, J. W. and Posewitz, M. C.},
abstractNote = {[FeFe]-hydrogenases (HYDA) link the production of molecular H{sub 2} to anaerobic metabolism in many green algae. Similar to Chlamydomonas reinhardtii, Chlorella variabilis NC64A (Trebouxiophyceae, Chlorophyta) exhibits [FeFe]-hydrogenase (HYDA) activity during anoxia. In contrast to C. reinhardtii and other chlorophycean algae, which contain hydrogenases with only the HYDA active site (H-cluster), C. variabilis NC64A is the only known green alga containing HYDA genes encoding accessory FeS cluster-binding domains (F-cluster). cDNA sequencing confirmed the presence of F-cluster HYDA1 mRNA transcripts, and identified deviations from the in silico splicing models. We show that HYDA activity in C. variabilis NC64A is coupled to anoxic photosynthetic electron transport (PSII linked, as well as PSII-independent) and dark fermentation. We also show that the in vivo H{sub 2}-photoproduction activity observed is as O2 sensitive as in C. reinhardtii. The two C. variabilis NC64A HYDA sequences are similar to homologs found in more deeply branching bacteria (Thermotogales), diatoms, and heterotrophic flagellates, suggesting that an F-cluster HYDA is the ancestral enzyme in algae. Phylogenetic analysis indicates that the algal HYDA H-cluster domains are monophyletic, suggesting that they share a common origin, and evolved from a single ancestral F-cluster HYDA. Furthermore, phylogenetic reconstruction indicates that the multiple algal HYDA paralogs are the result of gene duplication events that occurred independently within each algal lineage. Collectively, comparative genomic, physiological, and phylogenetic analyses of the C. variabilis NC64A hydrogenase has provided new insights into the molecular evolution and diversity of algal [FeFe]-hydrogenases.},
doi = {10.1007/s00425-011-1431-y},
journal = {Planta},
issn = {0032-0935},
number = 4,
volume = 234,
place = {United States},
year = {2011},
month = {10}
}