Evidence map›Paper›PMID 28186207›Full record

ArticleScientific reports2017

Complexity of the Ruminococcus flavefaciens FD-1 cellulosome reflects an expansion of family-related protein-protein interactions.

Vered Israeli-Ruimy, Pedro Bule, Sadanari Jindou, Bareket Dassa, Sarah Moraïs, Ilya Borovok, Yoav Barak, Michal Slutzki, Yuval Hamberg, Vânia Cardoso and 8 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-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

28 citing papers in PubMed, 48 citations in OpenAlex.

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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

18 authors at 6 institutions in 4 countries.

Vered Israeli-RuimyDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Pedro BuleCIISA - Faculdade de Medicina Veterinária, Universidade de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
Sadanari JindouDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.
Bareket DassaDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Sarah MoraïsDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Ilya BorovokDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.
Yoav BarakDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Michal SlutzkiDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Yuval HambergDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Vânia CardosoCIISA - Faculdade de Medicina Veterinária, Universidade de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
Victor D AlvesCIISA - Faculdade de Medicina Veterinária, Universidade de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
Shabir NajmudinCIISA - Faculdade de Medicina Veterinária, Universidade de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
Bryan A WhiteDepartment of Animal Sciences, Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Champaign, IL, USA.
Harry J FlintMicrobiology Group, Rowett Institute of Nutrition and Health, University of Aberdeen, Foresterhill, Aberdeen, Scotland, UK.
Harry J GilbertInstitute for Cell and Molecular Biosciences, Newcastle University, The Medical School, Newcastle upon Tyne NE2 4HH, UK.
Raphael LamedDepartment of Molecular Microbiology and Biotechnology, Tel Aviv University, Ramat Aviv, Israel.
Carlos M G A FontesCIISA - Faculdade de Medicina Veterinária, Universidade de Lisboa, Avenida da Universidade Técnica, 1300-477 Lisboa, Portugal.
Edward A BayerDepartment of Biomolecular Sciences, The Weizmann Institute of Science, Rehovot, Israel.
Weizmann Institute of Science · ILUniversity of Lisbon · PTTel Aviv University · ILNewcastle University · GBUniversity of Aberdeen · GBUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interactions play a vital role in cellular processes as exemplified by assembly of the intricate multi-enzyme cellulosome complex. Cellulosomes are assembled by selective high-affinity binding of enzyme-borne dockerin modules to repeated cohesin modules of structural proteins termed scaffoldins. Recent sequencing of the fiber-degrading Ruminococcus flavefaciens FD-1 genome revealed a particularly elaborate cellulosome system. In total, 223 dockerin-bearing ORFs potentially involved in cellulosome assembly and a variety of multi-modular scaffoldins were identified, and the dockerins were classified into six major groups. Here, extensive screening employing three complementary medium- to high-throughput platforms was used to characterize the different cohesin-dockerin specificities. The platforms included (i) cellulose-coated microarray assay, (ii) enzyme-linked immunosorbent assay (ELISA) and (iii) in-vivo co-expression and screening in Escherichia coli. The data revealed a collection of unique cohesin-dockerin interactions and support the functional relevance of dockerin classification into groups. In contrast to observations reported previously, a dual-binding mode is involved in cellulosome cell-surface attachment, whereas single-binding interactions operate for cellulosome integration of enzymes. This sui generis cellulosome model enhances our understanding of the mechanisms governing the remarkable ability of R. flavefaciens to degrade carbohydrates in the bovine rumen and provides a basis for constructing efficient nano-machines applied to biological processes.

Indexed as

Protein Interaction MapsAmino Acid SequenceBacterial ProteinsCell Cycle ProteinsCelluloseCellulosomesChromosomal Proteins, Non-HistoneCohesinsModels, BiologicalPhylogenyProtein Array AnalysisRuminococcusBacterial ProteinsCell Cycle ProteinsCelluloseChromosomal Proteins, Non-HistoneCohesins

Identifiers

PMID28186207
PMCPMC5301203
OpenAlexW2587444227

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.