Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein.
Biochemistry
; 57(1): 56-60, 2018 01 09.
Article
em En
| MEDLINE
| ID: mdl-29039649
ABSTRACT
Recent advances in proteomics and genomics have enabled discovery of thousands of previously nonannotated small open reading frames (smORFs) in genomes across evolutionary space. Furthermore, quantitative mass spectrometry has recently been applied to analysis of regulated smORF expression. However, bottom-up proteomics has remained relatively insensitive to membrane proteins, suggesting they may have been underdetected in previous studies. In this report, we add biochemical membrane protein enrichment to our previously developed label-free quantitative proteomics protocol, revealing a never-before-identified heat shock protein in Escherichia coli K12. This putative smORF-encoded heat shock protein, GndA, is likely to be â¼36-55 amino acids in length and contains a predicted transmembrane helix. We validate heat shock-regulated expression of the gndA smORF and demonstrate that a GndA-GFP fusion protein cofractionates with the cell membrane. Quantitative membrane proteomics therefore has the ability to reveal nonannotated small proteins that may play roles in bacterial stress responses.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Modelos Moleculares
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Fases de Leitura Aberta
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Resposta ao Choque Térmico
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Proteínas de Escherichia coli
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Escherichia coli K12
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Proteínas de Choque Térmico Pequenas
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Proteínas de Choque Térmico
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Proteínas de Membrana
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article