Evidence map›Paper›PMID 19820154›Full record

ArticleApplied and environmental microbiology2009

Effect of linker length and dockerin position on conversion of a Thermobifida fusca endoglucanase to the cellulosomal mode.

Jonathan Caspi, Yoav Barak, Rachel Haimovitz, Diana Irwin, Raphael Lamed, David B Wilson, Edward A Bayer

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Article
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  5. Creating a large designer cellulosome in yeast to boost ethanol production.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Carbohydrate Depolymerization by Intricate Cellulosomal Systems.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
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  10. Article
  11. Review
  12. Review
  13. Constructing a yeast to express the largest cellulosome complex on the cell surface.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. 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

7 authors at 3 institutions in 2 countries.

Jonathan CaspiDepartment of Biological Chemistry, The Weizmann Institute of Science, Rehovot 76100, Israel.
Yoav Barak
Rachel Haimovitz
Diana Irwin
Raphael Lamed
David B Wilson
Edward A Bayer
Weizmann Institute of Science · ILCornell University · USTel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have been developing the cellulases of Thermobifida fusca as a model to explore the conversion from a free cellulase system to the cellulosomal mode. Three of the six T. fusca cellulases (endoglucanase Cel6A and exoglucanases Cel6B and Cel48A) have been converted in previous work by replacing their cellulose-binding modules (CBMs) with a dockerin, and the resultant recombinant "cellulosomized" enzymes were incorporated into chimeric scaffolding proteins that contained cohesin(s) together with a CBM. The activities of the resultant designer cellulosomes were compared with an equivalent mixture of wild-type enzymes. In the present work, a fourth T. fusca cellulase, Cel5A, was equipped with a dockerin and intervening linker segments of different lengths to assess their contribution to the overall activity of simple one- and two-enzyme designer cellulosome complexes. The results demonstrated that cellulose binding played a major role in the degradation of crystalline cellulosic substrates. The combination of the converted Cel5A endoglucanase with the converted Cel48A exoglucanase also exhibited a measurable proximity effect for the most recalcitrant cellulosic substrate (Avicel). The length of the linker between the catalytic module and the dockerin had little, if any, effect on the activity. However, positioning of the dockerin on the opposite (C-terminal) side of the enzyme, consistent with the usual position of dockerins on most cellulosomal enzymes, resulted in an enhanced synergistic response. These results promote the development of more complex multienzyme designer cellulosomes, which may eventually be applied for improved degradation of plant cell wall biomass.

Indexed as

ActinomycetalesBacterial ProteinsCellulaseCelluloseCellulosomesProtein BindingProtein Interaction Domains and MotifsProtein Structure, TertiaryBacterial ProteinsCellulaseCelluloseendoglucanase Cel5A

Identifiers

PMID19820154
PMCPMC2786427
OpenAlexW2128898125

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.