Evidence map›Paper›PMID 9573155›Full record

ArticleJournal of bacteriology1998

In vitro and in vivo oxidation of methionine residues in small, acid-soluble spore proteins from Bacillus species.

C S Hayes, B Illades-Aguiar, L Casillas-Martinez, P Setlow

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
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  8. Structure of a protein-DNA complex essential for DNA protection in spores of Bacillus species.Proceedings of the National Academy of Sciences of the United States of America · 2008
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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

4 authors at 1 institution in 1 country.

C S HayesDepartment of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030, USA.
B Illades-Aguiar
L Casillas-Martinez
P Setlow
UConn Health · US

Funding

DEGRADATION REACTIONS IN SPORE GERMINATIONR01GM019698 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SETLOW, PETER · 1985 to 2007
$1.9M
DEGRADATION REACTIONS IN SPORE GERMINATIONR37GM019698 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SETLOW, PETER · 1994 to 2003
$1.7M
NIGMS NIH HHS GM19698NIGMS NIH HHS R01 GM019698NIGMS NIH HHS R37 GM019698
6 · The paper itself

Abstract

Methionine residues in alpha/beta-type small, acid-soluble spore proteins (SASP) of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (tBHP) or hydrogen peroxide (H2O2). These oxidized alpha/beta-type SASP no longer bound to DNA effectively, but DNA binding protected alpha/beta-type SASP against methionine oxidation by peroxides in vitro. Incubation of an oxidized alpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce methionine sulfoxide residues back to methionine, restored the alpha/beta-type SASP's ability to bind to DNA. Both tBHP and H2O2 caused some oxidation of the two methionine residues of an alpha/beta-type SASP (SspC) in spores of Bacillus subtilis, although one methionine which is highly conserved in alpha/beta-type SASP was only oxidized to a small degree. However, much more methionine sulfoxide was generated by peroxide treatment of spores carrying a mutant form of SspC which has a lower affinity for DNA. MsrA activity was present in wild-type B. subtilis spores. However, msrA mutant spores were no more sensitive to H2O2 than were wild-type spores. The major mechanism operating for dealing with oxidative damage to alpha/beta-type SASP in spores is DNA binding, which protects the protein's methionine residues from oxidation both in vitro and in vivo. This may be important in vivo since alpha/beta-type SASP containing oxidized methionine residues no longer bind DNA well and alpha/beta-type SASP-DNA binding is essential for long-term spore survival.

Indexed as

BacillusBacterial ProteinsMethionineOxidation-ReductionSpores, BacterialBacterial ProteinsMethionine

Identifiers

PMID9573155
PMCPMC107222
OpenAlexW2125517122

What OpenQuestion holds

Textmetadata
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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.