Evidence map›Paper›PMID 21866931›Full record

ArticleACS chemical biology2011

Small-molecule control of protein degradation using split adaptors.

Joseph H Davis, Tania A Baker, Robert T Sauer

Abstract read
In one paragraph

Article in ACS chemical biology, 2011. 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
0.7field-weighted citation impact, top 30% 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, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Protein overabundance is driven by growth robustness.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. The SspB adaptor drives structural changes in the AAA+ ClpXP protease during ssrA-tagged substrate delivery.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  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

3 authors at 2 institutions in 1 country.

Joseph H DavisDepartment of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Tania A Baker
Robert T Sauer
Massachusetts Institute of Technology · USHoward Hughes Medical Institute · US

Funding

REPRESSOR &ANTIREPRESSOR PROTEINS OF BACTERIOPHAGER01AI016892 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A, SAUER, ROBERT T · 1985 to 2022
$13.0M
Sequence Determinants of Protein Structure and StabilityR37AI015706 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2002 to 2011
$4.7M
Sequence Determinants of Protein Structure and StabilityR01GM101988 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2012 to 2019
$3.5M
NIAID NIH HHS AI-16892NIAID NIH HHS R01 AI016892NIAID NIH HHS R37 AI015706NIGMS NIH HHS R01 GM101988
6 · The paper itself

Abstract

Targeted intracellular degradation provides a method to study the biological function of proteins and has numerous applications in biotechnology. One promising approach uses adaptor proteins to target substrates with genetically encoded degradation tags for proteolysis. Here, we describe an engineered split-adaptor system, in which adaptor assembly and delivery of substrates to the ClpXP protease depends on a small molecule (rapamycin). This degradation system does not require modification of endogenous proteases, functions robustly over a wide range of adaptor concentrations, and does not require new synthesis of adaptors or proteases to initiate degradation. We demonstrate the efficacy of this system in E. coli by degrading tagged variants of LacI repressor and FtsA, an essential cell-division protein. In the latter case, addition of rapamycin causes pronounced filamentation because daughter cells cannot divide. Strikingly, washing rapamycin away reverses this phenotype. Our system is highly modular, with clearly defined interfaces for substrate binding, protease binding, and adaptor assembly, providing a clear path to extend this system to other degradation tags, proteases, or induction systems. Together, these new reagents should be useful in controlling protein degradation in bacteria.

Indexed as

Protein EngineeringEndopeptidase ClpEscherichia coliEscherichia coli ProteinsLac RepressorsMolecular WeightProteolysisRecombinant Fusion ProteinsSirolimusClpXP protease, E coliEndopeptidase ClpEscherichia coli ProteinsFtsA protein, E coliLacI protein, E coliLac RepressorsRecombinant Fusion ProteinsSirolimus

Identifiers

PMID21866931
PMCPMC3220803
OpenAlexW2147714441

What OpenQuestion holds

Textmetadata
LicenceTDM
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.