Evidence map›Paper›PMID 25059763›Full record

ArticleNature communications2014

Diverse and divergent protein post-translational modifications in two growth stages of a natural microbial community.

Zhou Li, Yingfeng Wang, Qiuming Yao, Nicholas B Justice, Tae-Hyuk Ahn, Dong Xu, Robert L Hettich, Jillian F Banfield, Chongle Pan

Abstract read
In one paragraph

Article in Nature communications, 2014. 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
–field-weighted citation impact
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.

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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

9 authors.

Zhou Li1] Computer Science and Mathematics Division and Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA [2] Graduate School of Genome Science and Technology, University of Tennessee-Oak Ridge National Laboratory, Knoxville, Tennessee 37996, USA.
Yingfeng WangComputer Science and Mathematics Division and Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA.
Qiuming YaoDepartment of Computer Science and Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, USA.
Nicholas B JusticeDepartment of Earth and Planetary Science, University of California, Berkeley, California 94720, USA.
Tae-Hyuk AhnComputer Science and Mathematics Division and Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA.
Dong XuDepartment of Computer Science and Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, Missouri 65211, USA.
Robert L Hettich1] Computer Science and Mathematics Division and Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA [2] Graduate School of Genome Science and Technology, University of Tennessee-Oak Ridge National Laboratory, Knoxville, Tennessee 37996, USA.
Jillian F BanfieldDepartment of Earth and Planetary Science, University of California, Berkeley, California 94720, USA.
Chongle Pan1] Computer Science and Mathematics Division and Chemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, USA [2] Graduate School of Genome Science and Technology, University of Tennessee-Oak Ridge National Laboratory, Knoxville, Tennessee 37996, USA.

Funding

Development of MUFOLD for Building High-Accuracy Protein Structure ModelsR01GM100701 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI XU, DONG · 2012 to 2016
$1.4M
NIGMS NIH HHS R01 GM100701NIGMS NIH HHS R01-GM100701
6 · The paper itself

Abstract

Detailed characterization of post-translational modifications (PTMs) of proteins in microbial communities remains a significant challenge. Here we directly identify and quantify a broad range of PTMs (hydroxylation, methylation, citrullination, acetylation, phosphorylation, methylthiolation, S-nitrosylation and nitration) in a natural microbial community from an acid mine drainage site. Approximately 29% of the identified proteins of the dominant Leptospirillum group II bacteria are modified, and 43% of modified proteins carry multiple PTM types. Most PTM events, except S-nitrosylations, have low fractional occupancy. Notably, PTM events are detected on Cas proteins involved in antiviral defense, an aspect of Cas biochemistry not considered previously. Further, Cas PTM profiles from Leptospirillum group II differ in early versus mature biofilms. PTM patterns are divergent on orthologues of two closely related, but ecologically differentiated, Leptospirillum group II bacteria. Our results highlight the prevalence and dynamics of PTMs of proteins, with potential significance for ecological adaptation and microbial evolution.

Indexed as

Protein Processing, Post-TranslationalAcetylationBacteriaBacterial ProteinsBiofilmsCaliforniaEcosystemEscherichia coliHydroxylationMethylationMicrobial ConsortiaPhosphorylationProteomeBacterial ProteinsProteome

Identifiers

PMID25059763
PMCPMC4279252

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.