Abstract:Comparative analysis of 15 complete cyanobacterial genome sequences, including ''near minimal'' genomes of five strains of Prochlorococcus spp., revealed 1,054 protein families [core cyanobacterial clusters of orthologous groups of proteins (core CyOGs)] encoded in at least 14 of them. The majority of the core CyOGs are involved in central cellular functions that are shared with other bacteria; 50 core CyOGs are specific for cyanobacteria, whereas 84 are exclusively shared by cyanobacteria and plants and͞or ot… Show more
“…However, lines of evidence from extant organismal physiology and Precambrian geochemical indicators corroborate the possibility that some rise in oxygen or other oxidized chemical species preceded the emergence of Form I Rubisco enzymes within cyanobacterial clades. Previous phylogenetic analyses indicate that anoxygenic photosynthetic lineages are more deeply rooted than oxygenic cyanobacterial lineages (Mulkidjanian et al., 2006; Xiong, 2007) and that cyanobacteria represent an evolutionary intermediate between anaerobic and obligate aerobic organisms (Harel, Karkar, Cheng, Falkowski, & Bhattacharya, 2015). Co‐evolution at organismal (i.e., the emergence or development of localized CO 2 or O 2 control volumes within cells) and protein (i.e., direct accumulation of mutations in sequences representing oxygen‐sensitive regions of proteins) levels may have been tightly coupled just prior to the GOE due to oxygen stresses and diminishing CO 2 availability in the near‐surface environment (Knoll, 2006; Tomitani et al., 2006).…”
Ribulose 1,5‐bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO, or Rubisco) catalyzes a key reaction by which inorganic carbon is converted into organic carbon in the metabolism of many aerobic and anaerobic organisms. Across the broader Rubisco protein family, homologs exhibit diverse biochemical characteristics and metabolic functions, but the evolutionary origins of this diversity are unclear. Evidence of the timing of Rubisco family emergence and diversification of its different forms has been obscured by a meager paleontological record of early Earth biota, their subcellular physiology and metabolic components. Here, we use computational models to reconstruct a Rubisco family phylogenetic tree, ancestral amino acid sequences at branching points on the tree, and protein structures for several key ancestors. Analysis of historic substitutions with respect to their structural locations shows that there were distinct periods of amino acid substitution enrichment above background levels near and within its oxygen‐sensitive active site and subunit interfaces over the divergence between Form III (associated with anoxia) and Form I (associated with oxia) groups in its evolutionary history. One possible interpretation is that these periods of substitutional enrichment are coincident with oxidative stress exerted by the rise of oxygenic photosynthesis in the Precambrian era. Our interpretation implies that the periods of Rubisco substitutional enrichment inferred near the transition from anaerobic Form III to aerobic Form I ancestral sequences predate the acquisition of Rubisco by fully derived cyanobacterial (i.e., dual photosystem‐bearing, oxygen‐evolving) clades. The partitioning of extant lineages at high clade levels within our Rubisco phylogeny indicates that horizontal transfer of Rubisco is a relatively infrequent event. Therefore, it is possible that the mutational enrichment periods between the Form III and Form I common ancestral sequences correspond to the adaptation of key oxygen‐sensitive components of Rubisco prior to, or coincident with, the Great Oxidation Event.
“…However, lines of evidence from extant organismal physiology and Precambrian geochemical indicators corroborate the possibility that some rise in oxygen or other oxidized chemical species preceded the emergence of Form I Rubisco enzymes within cyanobacterial clades. Previous phylogenetic analyses indicate that anoxygenic photosynthetic lineages are more deeply rooted than oxygenic cyanobacterial lineages (Mulkidjanian et al., 2006; Xiong, 2007) and that cyanobacteria represent an evolutionary intermediate between anaerobic and obligate aerobic organisms (Harel, Karkar, Cheng, Falkowski, & Bhattacharya, 2015). Co‐evolution at organismal (i.e., the emergence or development of localized CO 2 or O 2 control volumes within cells) and protein (i.e., direct accumulation of mutations in sequences representing oxygen‐sensitive regions of proteins) levels may have been tightly coupled just prior to the GOE due to oxygen stresses and diminishing CO 2 availability in the near‐surface environment (Knoll, 2006; Tomitani et al., 2006).…”
Ribulose 1,5‐bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO, or Rubisco) catalyzes a key reaction by which inorganic carbon is converted into organic carbon in the metabolism of many aerobic and anaerobic organisms. Across the broader Rubisco protein family, homologs exhibit diverse biochemical characteristics and metabolic functions, but the evolutionary origins of this diversity are unclear. Evidence of the timing of Rubisco family emergence and diversification of its different forms has been obscured by a meager paleontological record of early Earth biota, their subcellular physiology and metabolic components. Here, we use computational models to reconstruct a Rubisco family phylogenetic tree, ancestral amino acid sequences at branching points on the tree, and protein structures for several key ancestors. Analysis of historic substitutions with respect to their structural locations shows that there were distinct periods of amino acid substitution enrichment above background levels near and within its oxygen‐sensitive active site and subunit interfaces over the divergence between Form III (associated with anoxia) and Form I (associated with oxia) groups in its evolutionary history. One possible interpretation is that these periods of substitutional enrichment are coincident with oxidative stress exerted by the rise of oxygenic photosynthesis in the Precambrian era. Our interpretation implies that the periods of Rubisco substitutional enrichment inferred near the transition from anaerobic Form III to aerobic Form I ancestral sequences predate the acquisition of Rubisco by fully derived cyanobacterial (i.e., dual photosystem‐bearing, oxygen‐evolving) clades. The partitioning of extant lineages at high clade levels within our Rubisco phylogeny indicates that horizontal transfer of Rubisco is a relatively infrequent event. Therefore, it is possible that the mutational enrichment periods between the Form III and Form I common ancestral sequences correspond to the adaptation of key oxygen‐sensitive components of Rubisco prior to, or coincident with, the Great Oxidation Event.
“…A systematical IS element collection and IS family based classification system have been established by some professional databases, such as IS Finder (Siguier et al, 2006) and GenBank. Cyanobacteria, considered as the ancestor of photosynthetic organisms on the earth, consist of large groups of organisms from unicellular to filamentous forms (Mulkidjanian et al, 2006). However, less is known about the transposable elements in cyanobacteria.…”
“…In oxygenic cyanobacteria, photosystem I (PSI) strips electrons from chlorophyll to generate energy and reductants (ATP and NADPH), while a second photosystem (PSII), assisted by a Mn-based catalytic complex, replenishes the electron pool by oxidizing H 2 O to O 2 (21). In contrast, green and purple sulfur bacteria (anoxygenic photoautotrophs) commonly use sulfide to drive primary production with PSI-and PSII-like machinery, respectively (22,23). In this case, the production of oxidized sulfur compounds (S 0 or SO 4 ), rather than O 2 , balances the formation of OM.…”
Molecular oxygen (O2) began to accumulate in the atmosphere and surface ocean ca. 2,400 million years ago (Ma), but the persistent oxygenation of water masses throughout the oceans developed much later, perhaps beginning as recently as 580 -550 Ma. For much of the intervening interval, moderately oxic surface waters lay above an oxygen minimum zone (OMZ) that tended toward euxinia (anoxic and sulfidic). Here we illustrate how contributions to primary production by anoxygenic photoautotrophs (including physiologically versatile cyanobacteria) influenced biogeochemical cycling during Earth's middle age, helping to perpetuate our planet's intermediate redox state by tempering O 2 production. Specifically, the ability to generate organic matter (OM) using sulfide as an electron donor enabled a positive biogeochemical feedback that sustained euxinia in the OMZ. On a geologic time scale, pyrite precipitation and burial governed a second feedback that moderated sulfide availability and water column oxygenation. Thus, we argue that the proportional contribution of anoxygenic photosynthesis to overall primary production would have influenced oceanic redox and the Proterozoic O 2 budget. Later Neoproterozoic collapse of widespread euxinia and a concomitant return to ferruginous (anoxic and Fe 2؉ rich) subsurface waters set in motion Earth's transition from its prokaryote-dominated middle age, removing a physiological barrier to eukaryotic diversification (sulfide) and establishing, for the first time in Earth's history, complete dominance of oxygenic photosynthesis in the oceans. This paved the way for the further oxygenation of the oceans and atmosphere and, ultimately, the evolution of complex multicellular organisms.ocean chemistry ͉ primary production ͉ Proterozoic biosphere
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