Evidence map›Paper›PMID 18199753›Full record

ArticleThe Journal of biological chemistry2008

Biogenesis of phycobiliproteins: II. CpcS-I and CpcU comprise the heterodimeric bilin lyase that attaches phycocyanobilin to CYS-82 OF beta-phycocyanin and CYS-81 of allophycocyanin subunits in Synechococcus sp. PCC 7002.

Nicolle A Saunée, Shervonda R Williams, Donald A Bryant, Wendy M Schluchter

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  9. Article
  10. Molecular bases of an alternative dual-enzyme system for light color acclimation of marineProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020
    Review
  12. 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
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Adaptation to Blue Light in MarineFrontiers in microbiology · 2017
    Article
  19. Article
  20. Structure and mechanism of the phycobiliprotein lyase CpcT.The Journal of biological chemistry · 2014
    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

4 authors at 2 institutions in 1 country.

Nicolle A SaunéeDepartment of Biological Sciences, University of New Orleans, New Orleans, Louisiana 70148, USA
Shervonda R Williams
Donald A Bryant
Wendy M Schluchter
University of New Orleans · USPennsylvania State University · US

Funding

REGULATION OF BILIPROTEIN IN CYANOBACTERIAR01GM031625 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BRYANT, DONALD A · 1985 to 2002
$797k
NIGMS NIH HHS GM-31625
6 · The paper itself

Abstract

The Synechococcus sp. PCC 7002 genome encodes three genes, denoted cpcS-I, cpcU, cpcV, with sequence similarity to cpeS. CpcS-I copurified with His(6)-tagged (HT) CpcU as a heterodimer, CpcSU. When CpcSU was assayed for bilin lyase activity in vitro with phycocyanobilin (PCB) and apophycocyanin, the reaction product had an absorbance maximum of 622 nm and was highly fluorescent (lambda(max) = 643 nm). In control reactions with PCB and apophycocyanin, the products had absorption maxima at 635 nm and very low fluorescence yields, indicating they contained the more oxidized mesobiliverdin (Arciero, D. M., Bryant, D. A., and Glazer, A. N. (1988) J. Biol. Chem. 263, 18343-18349). Tryptic peptide mapping showed that the CpcSU-dependent reaction product had one major PCB-containing peptide that contained the PCB binding site Cys-82. The CpcSU lyase was also tested with recombinant apoHT-allophycocyanin (aporHT-AP) and PCB in vitro. AporHT-AP formed an ApcA/ApcB heterodimer with an apparent mass of approximately 27 kDa. When aporHT-AP was incubated with PCB and CpcSU, the product had an absorbance maximum of 614 nm and a fluorescence emission maximum at 636 nm, the expected maxima for monomeric holo-AP. When no enzyme or CpcS-I or CpcU was added alone, the products had absorbance maxima between 645 and 647 nm and were not fluorescent. When these reaction products were analyzed by gel electrophoresis and zinc-enhanced fluorescence emission, only the reaction products from CpcSU had PCB attached to both AP subunits. Therefore, CpcSU is the bilin lyase-responsible for attachment of PCB to Cys-82 of CpcB and Cys-81 of ApcA and ApcB.

Indexed as

Bacterial ProteinsLyasesPhycobilinsPhycocyaninSynechococcusallophycocyaninBacterial ProteinsLyasesPhycobilinsPhycocyaninphycocyanin alpha-subunit phycocyanobilin lyasephycocyanobilin

Identifiers

PMID18199753
PMCPMC2276331
OpenAlexW1968729463

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.