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
Language
- eng
Conference Location
- United States