Evidence map›Paper›PMID 20876568›Full record

ArticleThe Journal of biological chemistry2010

CpeS is a lyase specific for attachment of 3Z-PEB to Cys82 of {beta}-phycoerythrin from Prochlorococcus marinus MED4.

Jessica Wiethaus, Andrea W U Busch, Klaus Kock, Lars I Leichert, Christian Herrmann, Nicole Frankenberg-Dinkel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
1.5field-weighted citation impact, top 19% 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, 28 citations in OpenAlex.

  1. Article
  2. Draft Genome Sequences ofJournal of genomics · 2023
    Article
  3. Review
  4. Interplay between differentially expressed enzymes contributes to light color acclimation in marineProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. Adaptation to Blue Light in MarineFrontiers in microbiology · 2017
    Article
  7. Article
  8. Article
  9. Article
  10. Phycoerythrin-specific bilin lyase-isomerase controls blue-green chromatic acclimation in marine Synechococcus.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Article
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

6 authors at 3 institutions in 3 countries.

Jessica WiethausDepartment of Physiology of Microorganisms, Faculty of Biology and Biotechnology, Ruhr-University Bochum, Universitaetsstrasse 150, 44780 Bochum, Germany.
Andrea W U Busch
Klaus Kock
Lars I Leichert
Christian Herrmann
Nicole Frankenberg-Dinkel
Ruhr University Bochum · DEDepartment of Physics, Mathematics and Informatics · BYG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In contrast to the majority of cyanobacteria, the unicellular marine cyanobacterium Prochlorococcus marinus MED4 uses an intrinsic divinyl-chlorophyll-dependent light-harvesting system for photosynthesis. Despite the absence of phycobilisomes, this high-light adapted strain possesses β-phycoerythrin (CpeB), an S-type lyase (CpeS), and enzymes for the biosynthesis of phycoerythrobilin (PEB) and phycocyanobilin. Of all linear tetrapyrroles synthesized by Prochlorococcus including their 3Z- and 3E-isomers, CpeS binds both isomers of PEB and its biosynthetic precursor 15,16-dihydrobiliverdin (DHBV). However, dimerization of CpeS is independent of bilins, which are tightly bound in a complex at a ratio of 1:1. Although bilin binding by CpeS is fast, transfer to CpeB is rather slow. CpeS is able to attach 3E-PEB and 3Z-PEB to dimeric CpeB but not DHBV. CpeS transfer of 3Z-PEB exclusively yields correctly bound βCys(82)-PEB, whereas βCys(82)-DHBV is a side product of 3E-PEB transfer. Spontaneous 3E- and 3Z-PEB addition to CpeB is faulty, and products are in both cases βCys(82)-DHBV and likely a PEB bound at βCys(82) in a non-native configuration. Our data indicate that CpeS is specific for 3Z-PEB transfer to βCys(82) of phycoerythrin and essential for the correct configuration of the attachment product.

Indexed as

Amino Acid MotifsBacterial ProteinsIsomerismLyasesPhycobilinsPhycoerythrinProchlorococcusProtein BindingBacterial ProteinsLyasesPhycobilinsPhycoerythrinphycoerythrobilin

Identifiers

PMID20876568
PMCPMC2988361
OpenAlexW2058029566

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.