Comparative Membrane Proteomics Reveals a Nonannotated E. coli Heat Shock Protein.

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 ∼36-55 amino acids in length and contains a predicted transmembrane h

SUBMITTER: Yuan P 

PROVIDER: S-EPMC5761644 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature