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Titolo:
Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry
Autore:
Kelleher, NL; Taylor, SV; Grannis, D; Kinsland, C; Chiu, HJ; Begley, TP; McLafferty, FW;
Indirizzi:
Cornell Univ, Baker Lab, Dept Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 ker Lab, Dept Chem, Ithaca, NY 14853 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 8, volume: 7, anno: 1998,
pagine: 1796 - 1801
SICI:
0961-8368(199808)7:8<1796:ESAOTS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
MULTIPLY-CHARGED IONS; INFRARED MULTIPHOTON DISSOCIATION; DNA-SEQUENCE; ELECTROSPRAY; SPECTRA; PROTEINS; GENOME; MOLECULES; ACCURACY; K-12;
Keywords:
electrospray; Escherichia coli; Fourier-transform mass spectrometry; operon; sequence; thiamin biosynthesis; thiCEFSGH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: McLafferty, FW Cornell Univ, Baker Lab, Dept Chem, Ithaca, NY 14853 USA Cornell Univ Ithaca NY USA 14853 hem, Ithaca, NY 14853 USA
Citazione:
N.L. Kelleher et al., "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry", PROTEIN SCI, 7(8), 1998, pp. 1796-1801

Abstract

The 10(5) resolving power and MS/MS capabilities of Fourier-transform massspectrometry provide electrospray ionization mass spectra containing >100 molecular and fragment ion moss values of high accuracy, Applying these spectra to the detection and localization of errors and modifications in the DNA-derived sequences of proteins is illustrated with the thiCEFSGH thiamin biosynthesis operon from Escherichia coli. Direct fragmentation of the multiply-charged intact protein inns produces large fragment ions covering the entire sequence; further dissociation of these fragment ions provides information on their sequences. For ThiE (23 kDa), the entire sequence was verified in a single spectrum with an accurate (0.3 Da) molecular weight (M-r) value, with confirmation from MS/MS fragment masses. Those for ThiH (46 kDa)showed that the M-r value (1 Da error) represented the protein without thestart Met residue, For ThiF (27 kDa), MS/MS localized a sequence discrepancy to a 34 residue peptide, The first 107 residues of ThiC (74 kDa) were shown to be correct, with C-terminal heterogeneity indicated. For ThiG (predicted M-r = 34 kDa), ESI/FTMS showed two components of 7,310.74 (ThiS) and 26,896.5 Da (ThiG); MS/MS uncovered three reading frame errors and a stop codon for the first protein. MS/MS ions are consistent with 68 fragments predicted by the corrected ThiS/ThiG DNA sequences.

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Documento generato il 12/07/20 alle ore 06:21:32