Evidence map›Paper›PMID 17921310›Full record

ArticleJournal of bacteriology2007

Rhodobacter capsulatus OlsA is a bifunctional enzyme active in both ornithine lipid and phosphatidic acid biosynthesis.

Semra Aygun-Sunar, Rahmi Bilaloglu, Howard Goldfine, Fevzi Daldal

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Phosphatidic acid synthesis in bacteria.Biochimica et biophysica acta · 2013
    Review
  10. Review
  11. Article
  12. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Semra Aygun-SunarDepartment of Biology, University of Pennsylvania, 433 S. University Ave., Philadelphia, PA 19104, USA.
Rahmi Bilaloglu
Howard Goldfine
Fevzi Daldal
University of Pennsylvania · USBursa Uludağ Üni̇versi̇tesi̇ · TR

Funding

Respiratory Complex III: Supercomplexes and ROS, from Bacteria to HumanR01GM038237 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DALDAL, M. FEVZI · 1987 to 2018
$5.9M
PHOSPHOLIPASES AND THE PATHOGENESIS OF LISTERIA MONOCYTOR01AI045153 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI GOLDFINE, HOWARD · 2000 to 2004
$1.4M
NIAID NIH HHS AI45153NIAID NIH HHS R01 AI045153NIGMS NIH HHS GM38237NIGMS NIH HHS R01 GM038237
6 · The paper itself

Abstract

The Rhodobacter capsulatus genome contains three genes (olsA [plsC138], plsC316, and plsC3498) that are annotated as lysophosphatidic acid (1-acyl-sn-glycerol-3-phosphate) acyltransferase (AGPAT). Of these genes, olsA was previously shown to be an O-acyltransferase in the second step of ornithine lipid biosynthesis, which is important for optimal steady-state levels of c-type cytochromes (S. Aygun-Sunar, S. Mandaci, H.-G. Koch, I. V. J. Murray, H. Goldfine, and F. Daldal. Mol. Microbiol. 61:418-435, 2006). The roles of the remaining plsC316 and plsC3498 genes remained unknown. In this work, these genes were cloned, and chromosomal insertion-deletion mutations inactivating them were obtained to define their function. Characterization of these mutants indicated that, unlike the Escherichia coli plsC, neither plsC316 nor plsC3498 was essential in R. capsulatus. In contrast, no plsC316 olsA double mutant could be isolated, indicating that an intact copy of either olsA or plsC316 was required for R. capsulatus growth under the conditions tested. Compared to OlsA null mutants, PlsC316 null mutants contained ornithine lipid and had no c-type cytochrome-related phenotype. However, they exhibited slight growth impairment and highly altered total fatty acid and phospholipid profiles. Heterologous expression in an E. coli plsC(Ts) mutant of either R. capsulatus plsC316 or olsA gene products supported growth at a nonpermissive temperature, exhibited AGPAT activity in vitro, and restored phosphatidic acid biosynthesis. The more vigorous AGPAT activity displayed by PlsC316 suggested that plsC316 encodes the main AGPAT required for glycerophospholipid synthesis in R. capsulatus, while olsA acts as an alternative AGPAT that is specific for ornithine lipid synthesis. This study therefore revealed for the first time that some OlsA enzymes, like the enzyme of R. capsulatus, are bifunctional and involved in both membrane ornithine lipid and glycerophospholipid biosynthesis.

Indexed as

1-Acylglycerol-3-Phosphate O-AcyltransferaseAmino Acid SequenceBacterial ProteinsCytochromes cGene Expression Regulation, BacterialGlycerol-3-Phosphate O-AcyltransferaseGlycerophospholipidsLipidsMolecular Sequence DataMutationOpen Reading FramesOrnithinePhosphatidic AcidsRhodobacter capsulatus1-Acylglycerol-3-Phosphate O-AcyltransferaseBacterial ProteinsCytochromes cGlycerol-3-Phosphate O-AcyltransferaseGlycerophospholipidsLipidsOrnithineornithine containing aminolipidPhosphatidic Acids

Identifiers

PMID17921310
PMCPMC2168953
OpenAlexW2138116635

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.