Evidence map›Paper›PMID 35351518›Full record

ArticleJournal of molecular biology2022

How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein.

Alexander G Kozlov, Xian Cheng, Hongshan Zhang, Min Kyung Shinn, Elizabeth Weiland, Binh Nguyen, Irina A Shkel, Emily Zytkiewicz, Ilya J Finkelstein, M Thomas Record and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2022. 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
4.0field-weighted citation impact, top 5% 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.

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  20. Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 3 institutions in 1 country.

Alexander G KozlovDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, United States.
Xian ChengDepartments of Chemistry and Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
Hongshan ZhangDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, United States.
Min Kyung ShinnDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, United States; Department of Biomedical Engineering, Center for Science & Engineering of Living Systems (CSELS), Washington University in St. Louis, St. Louis, MO 63130, United States.
Elizabeth WeilandDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, United States.
Binh NguyenDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, United States.
Irina A ShkelDepartments of Chemistry and Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
Emily ZytkiewiczDepartments of Chemistry and Biochemistry, University of Wisconsin, Madison, WI 53706, United States.
Ilya J FinkelsteinDepartment of Molecular Biosciences and Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, TX 78712, United States.
M Thomas RecordDepartments of Chemistry and Biochemistry, University of Wisconsin, Madison, WI 53706, United States. Electronic address: mtrecord@wisc.edu.
Timothy M LohmanDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110, United States. Electronic address: lohman@wustl.edu.
Washington University in St. Louis · USUniversity of Wisconsin–Madison · USThe University of Texas at Austin · US

Funding

SSB PROTEIN/DNA INTERACTIONSR01GM030498 · NIGMS · WASHINGTON UNIVERSITY · PI LOHMAN, TIMOTHY M · 1985 to 2019
$7.4M
Mechanisms of Helicases, Translocases and SSB Proteins involved in Genome MaintenanceR35GM136632 · NIGMS · WASHINGTON UNIVERSITY · PI Timothy M Lohman · 2020 to 2026
$5.5M
Mechanisms of RNA Polymerase-Promoter and lac Repressor-Operator InteractionsR35GM118100 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI RECORD, M. THOMAS · 2016 to 2020
$2.6M
NIGMS NIH HHS R01 GM030498NIGMS NIH HHS R35 GM118100NIGMS NIH HHS R35 GM136632
6 · The paper itself

Abstract

E. coli single-stranded-DNA binding protein (EcSSB) displays nearest-neighbor (NN) and non-nearest-neighbor (NNN)) cooperativity in binding ssDNA during genome maintenance. NNN cooperativity requires the intrinsically-disordered linkers (IDL) of the C-terminal tails. Potassium glutamate (KGlu), the primary E. coli salt, promotes NNN-cooperativity, while KCl inhibits it. We find that KGlu promotes compaction of a single polymeric SSB-coated ssDNA beyond what occurs in KCl, indicating a link of compaction to NNN-cooperativity. EcSSB also undergoes liquid-liquid phase separation (LLPS), inhibited by ssDNA binding. We find that LLPS, like NNN-cooperativity, is promoted by increasing [KGlu] in the physiological range, while increasing [KCl] and/or deletion of the IDL eliminate LLPS, indicating similar interactions in both processes. From quantitative determinations of interactions of KGlu and KCl with protein model compounds, we deduce that the opposing effects of KGlu and KCl on SSB LLPS and cooperativity arise from their opposite interactions with amide groups. KGlu interacts unfavorably with the backbone (especially Gly) and side chain amide groups of the IDL, promoting amide-amide interactions in LLPS and NNN-cooperativity. By contrast, KCl interacts favorably with these amide groups and therefore inhibits LLPS and NNN-cooperativity. These results highlight the importance of salt interactions in regulating the propensity of proteins to undergo LLPS.

Indexed as

DNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsGlutamic AcidAmidesPhase TransitionProtein BindingAmidesDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsGlutamic AcidSSB protein, E colibiomolecular condensatesDNA replicationLiquid-liquid phase separationsalt effectssingle molecule DNA collapse

Identifiers

PMID35351518
PMCPMC9400470
OpenAlexW4220746620

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.