Evidence map›Paper›PMID 17618403›Full record

ArticleExtremophiles : life under extreme conditions2007

Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella livingstonensis Ac10, for global identification of cold-inducible proteins.

Jun Kawamoto, Tatsuo Kurihara, Masanari Kitagawa, Ikunoshin Kato, Nobuyoshi Esaki

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Article in Extremophiles : life under extreme conditions, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

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21citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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.

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3 · Its place in the literature

Who cites it

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Psychrophiles: A journey of hope.Journal of biosciences · 2021
    Review
  6. Adaptation of the Marine BacteriumInternational journal of molecular sciences · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Jun KawamotoInstitute for Chemical Research, Kyoto University, Uji, Kyoto, 611-0011, Japan.
Tatsuo Kurihara
Masanari Kitagawa
Ikunoshin Kato
Nobuyoshi Esaki

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteomic analysis of a cold-adapted bacterium, Shewanella livingstonensis Ac10, isolated from Antarctic seawater was carried out to elucidate its cold-adaptation mechanism. The cells were grown at 4 degrees C and 18 degrees C, and soluble and membrane proteins were analyzed by two-dimensional gel electrophoresis. At 4 degrees C, the relative abundance of 47 soluble proteins and five membrane proteins increased more than twofold, and these proteins were analyzed by peptide mass fingerprinting. Twenty-six soluble proteins and two membrane proteins were identified. These included proteins involved in RNA synthesis and folding (RpoA, GreA, and CspA), protein synthesis and folding (TufB, Efp, LysU, and Tig), membrane transport (OmpA and OmpC), and motility (FlgE and FlgL). Cold-inducible RpoA, GreA, and CspA may be required for efficient and accurate transcription and proper folding of RNA at low temperatures, where base pairing of nucleic acids is stable and undesired secondary structures of RNA tend to form. Tig is supposed to have peptidyl-prolyl cis-trans isomerase activity and facilitate proper folding of proteins at low temperatures. The cold induction of OmpA and OmpC is likely to counteract the low diffusion rate of solutes at low temperatures and enables the efficient uptake of nutrients. These results provided many clues to understand microbial cold-adaptation mechanisms.

Indexed as

Adaptation, PhysiologicalCold TemperatureProteomicsAntarctic RegionsBacterial ProteinsElectrophoresis, Gel, Two-DimensionalGene Expression Regulation, BacterialPeptide MappingRNA, BacterialRNA, MessengerSeawaterShewanellaTime FactorsTranscription, GeneticWater MicrobiologyBacterial ProteinsRNA, BacterialRNA, Messenger

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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.