Identification of a chloroform-soluble membrane miniprotein in Escherichia coli and its homolog in Salmonella typhimurium.

Journal Article (Journal Article)

Two homologous 29 amino acid-long highly hydrophobic membrane miniproteins were identified in the Bligh-Dyer lipid extracts of Escherichia coli and Salmonella typhimurium using liquid chromatography/tandem mass spectrometry (LC/MS/MS). The amino acid sequences of the proteins were determined by collision-induced dissociation tandem mass spectrometry, in conjunction with a translating BLAST (tBLASTn) search, i.e., comparing the MS/MS-determined protein query sequence against the six-frame translations of the nucleotide sequences of the E. coli and S. typhimurium genomes. Further MS characterization revealed that both proteins retain the N-terminal initiating formyl-methionines. The methodologies described here may be amendable for detecting and characterizing small hydrophobic proteins in other organisms that are difficult to annotate or analyze by conventional methods.

Full Text

Duke Authors

Cited Authors

  • Guan, Z; Wang, X; Raetz, CRH

Published Date

  • February 15, 2011

Published In

Volume / Issue

  • 409 / 2

Start / End Page

  • 284 - 289

PubMed ID

  • 21050835

Pubmed Central ID

  • PMC3018292

Electronic International Standard Serial Number (EISSN)

  • 1096-0309

Digital Object Identifier (DOI)

  • 10.1016/j.ab.2010.10.035


  • eng

Conference Location

  • United States