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Originally published In Press as doi:10.1074/jbc.M008342200 on April 17, 2001

J. Biol. Chem., Vol. 276, Issue 30, 28327-28339, July 27, 2001
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Functional Assignment of the 20 S Proteasome from Trypanosoma brucei Using Mass Spectrometry and New Bioinformatics Approaches*

Lan HuangDagger , Richard J. JacobDagger , Scott C.-H. PeggDagger , Michael A. BaldwinDagger , Ching C. WangDagger , Alma L. BurlingameDagger , and Patricia C. BabbittDagger §

From the Dagger  Department of Pharmaceutical Chemistry and the § Department of Biopharmaceutical Sciences, University of California, San Francisco, California 94143

As experimental technologies for characterization of proteomes emerge, bioinformatic analysis of the data becomes essential. Separation and identification technologies currently based on two-dimensional gels/mass spectrometry provide the inherent analytical power required. This strategy involves protein spot digestion and accurate mass mapping together with computational interrogation of available data bases for protein functional identification. When either no exact match is found or when the possible matches only partially account for molecular weights actually observed, peptide sequencing by tandem mass spectrometry has emerged as the methodology of choice to provide the basic additional information required. To evaluate the capabilities of bioinformatics methods employed for identifying homologs of a protein of interest, we attempted to identify the major proteins from the 20 S proteasome of Trypanosoma brucei using sequence information determined using mass spectrometry. The results suggest that neither the traditional query engines, BLAST and FASTA, nor specialized software developed for analysis of sequence information obtained by mass spectrometry are able to identify even closely related sequences at statistically significant scores. To address this deficit, new bioinformatics approaches were developed for concomitant use of the multiple fragments of short sequence typically available from methods of tandem mass spectrometry. These approaches rely on the occurrence of congruence across searches of multiple fragments from a single protein. This method resulted in sharply better statistical significance values for correct hits in the data base output relative to that achieved for independent searches using single sequence fragments.

* The mass spectrometry performed at the University of California, San Francisco, Mass Spectrometry Facility, was supported by National Institutes of Health Grant NCRR RR01614 (to A. L. B.), bioinformatics was supported by National Institutes of Health Grant RO1 GM60595 (to P. C. B.), and biochemistry was supported by National Institutes of Health Grant R01 AI21786 (to C. C. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF198386, AF148125, AF198387, AF169652, AF140353, AJ131148, AF169651, AJ131043, AJ130820, AF169653, AF226673, AF226674, AF148124, AF290945.

To whom correspondence should be addressed. Tel.: 415-476-3784; Fax: 415-476-0688; E-mail: babbitt@cgl.ucsf.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.