Evidence map›Paper›PMID 26174026›Full record

ArticlePhotosynthesis research2016

Evidence for the presence of key chlorophyll-biosynthesis-related proteins in the genus Rubrobacter (Phylum Actinobacteria) and its implications for the evolution and origin of photosynthesis.

Radhey S Gupta, Bijendra Khadka

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Article in Photosynthesis research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 30 citations in OpenAlex.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Radhey S GuptaDepartment of Biochemistry, McMaster University, Hamilton, ON, L8N 3Z5, Canada. gupta@mcmaster.ca.
Bijendra KhadkaDepartment of Biochemistry, McMaster University, Hamilton, ON, L8N 3Z5, Canada.
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homologs showing high degree of sequence similarity to the three subunits of the protochlorophyllide oxidoreductase enzyme complex (viz. BchL, BchN, and BchB), which carries out a central role in chlorophyll-bacteriochlorophyll (Bchl) biosynthesis, are uniquely found in photosynthetic organisms. The results of BLAST searches and homology modeling presented here show that proteins exhibiting a high degree of sequence and structural similarity to the BchB and BchN proteins are also present in organisms from the high G+C Gram-positive phylum of Actinobacteria, specifically in members of the genus Rubrobacter (R. x ylanophilus and R. r adiotolerans). The results presented exclude the possibility that the observed BLAST hits are for subunits of the nitrogenase complex or the chlorin reductase complex. The branching in phylogenetic trees and the sequence characteristics of the Rubrobacter BchB/BchN homologs indicate that these homologs are distinct from those found in other photosynthetic bacteria and that they may represent ancestral forms of the BchB/BchN proteins. Although a homolog showing high degree of sequence similarity to the BchL protein was not detected in Rubrobacter, another protein, belonging to the ParA/Soj/MinD family, present in these bacteria, exhibits high degree of structural similarity to the BchL. In addition to the BchB/BchN homologs, Rubrobacter species also contain homologs showing high degree of sequence similarity to different subunits of magnesium chelatase (BchD, BchH, and BchI) as well as proteins showing significant similarity to the BchP and BchG proteins. Interestingly, no homologs corresponding to the BchX, BchY, and BchZ proteins were detected in the Rubrobacter species. These results provide the first suggestive evidence that some form of photosynthesis either exists or was anciently present within the phylum Actinobacteria (high G+C Gram-positive) in members of the genus Rubrobacter. The significance of these results concerning the origin of the Bchl-based photosynthesis is also discussed.

Indexed as

Biological EvolutionPhotosynthesisActinobacteriaAmino Acid SequenceBacterial ProteinsChlorophyllCrystallography, X-RayLikelihood FunctionsModels, MolecularMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsPhylogenyProtein SubunitsReproducibility of ResultsSequence AlignmentSequence Homology, Amino AcidBacterial ProteinsChlorophyllOxidoreductases Acting on CH-CH Group DonorsProtein Subunitsprotochlorophyllide reductaseBchL-B-N homologsChlorophyll-bacteriochlorophyll (Bchl) biosynthesisGenus Rubrobacter (phylum Actinobacteria)Origin of photosynthesisParA-MinD proteinsPhotosynthetic phyla of bacteria

Identifiers

PMID26174026
OpenAlexW1243786322

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.