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Frequent-subsequence-based prediction of outer membrane proteins
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Source International Conference on Knowledge Discovery and Data Mining archive
Proceedings of the ninth ACM SIGKDD international conference on Knowledge discovery and data mining table of contents
Washington, D.C.
SESSION: Industrial/government track table of contents
Pages: 436 - 445  
Year of Publication: 2003
ISBN:1-58113-737-0
Authors
Rong She  Simon Fraser University
Fei Chen  Simon Fraser University
Ke Wang  Simon Fraser University
Martin Ester  Simon Fraser University
Jennifer L. Gardy  Simon Fraser University
Fiona S. L. Brinkman  Simon Fraser University
Sponsors
SIGKDD: ACM Special Interest Group on Knowledge Discovery in Data
SIGMOD: ACM Special Interest Group on Management of Data
Publisher
ACM  New York, NY, USA
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ABSTRACT

A number of medically important disease-causing bacteria (collectively called Gram-negative bacteria) are noted for the extra "outer" membrane that surrounds their cell. Proteins resident in this membrane (outer membrane proteins, or OMPs) are of primary research interest for antibiotic and vaccine drug design as they are on the surface of the bacteria and so are the most accessible targets to develop new drugs against. With the development of genome sequencing technology and bioinformatics, biologists can now deduce all the proteins that are likely produced in a given bacteria and have attempted to classify where proteins are located in a bacterial cell. However such protein localization programs are currently least accurate when predicting OMPs, and so there is a current need for the development of a better OMP classifier. Data mining research suggests that the use of frequent patterns has good performance in aiding the development of accurate and efficient classification algorithms. In this paper, we present two methods to identify OMPs based on frequent subsequences and test them on all Gram-negative bacterial proteins whose localizations have been determined by biological experiments. One classifier follows an association rule approach, while the other is based on support vector machines (SVMs). We compare the proposed methods with the state-of-the-art methods in the biological domain. The results demonstrate that our methods are better both in terms of accurately identifying OMPs and providing biological insights that increase our understanding of the structures and functions of these important proteins.


REFERENCES

Note: OCR errors may be found in this Reference List extracted from the full text article. ACM has opted to expose the complete List rather than only correct and linked references.

 
1
Ali K., Manganaris S. and Srikant R., Partial classification using association rules, KDD'97, p. 115--118, 1997.
 
2
Boeckmann B., Bairoch A., Apweiler R., Blatter M.-C., Estreicher A., Gasteiger E., Martin M. J., Michoud K., O'Donovan C., Phan I., Pilbout S., Schneider M. The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003, Nucleic Acids Res. 31:365--370, 2003.
 
3
 
4
Diederichs K., Freigang J., Umhau S., Zeth K. and Breed J., Prediction by a neural network of outer membrane β-strand topology, Protein Science, 7, p. 2413--2420, 1998.
 
5
Eisenhaber F. and Bork P., Wanted: subcellular localization of proteins based on sequences, Trends in Cell Biology, 8, p. 169--170, 1998.
 
6
Hua S. and Sun Z., Support vector machine approach for protein subcellular localization prediction, Bioinformatics, 17(8), p. 721--728, 2001.
 
7
 
8
Jacoboni I., Martelli P., Fariselli P., De Pinto V. and Casadio R., Prediction of the transmembrane regions of β-barrel membrane proteins with a neural network-based predictor, Protein Science, 10, p. 779--787, 2001.
 
9
Joachims T., Learning to Classify Text Using Support Vector Machines. Dissertation, Kluwer, 2002. software downloadable at http://svmlight.joachims.org/
 
10
11
 
12
Leslie C., Eskin E. and Noble W., The spectrum kernel: A string kernel for SVM protein classification, Proceedings of the Pacific Symposium on Biocomputing, p. 564--575, 2002.
 
13
Liu B., Hsu W. and Ma Y., Integrating classification and association rule mining, KDD'98, New York, NY, 1998.
 
14
Martelli P., Fariselli P., Krogh A. and Casadio R., A sequence-profile-based HMM for predicting and discrimating β barrel membrane proteins, Bioinformatics, 18(1) 2002, S46-S53, 2002.
 
15
Nakashima H. and Nishikawa K., Discrimination of intracellular and extracellular proteins using amino acid composition and residue-pair frequencies, Journal of Molecular Biology, 238, p. 54--61, 1994.
 
16
 
17
Reinhardt A. and Hubbard T., Using neural networks for prediction of the subcellular location of proteins, Nucleic Acids Research, 26(9), p. 2230--2236, 1998.
 
18
Rulequest Research, Information on See5/C5.0, at <u>http://www.rulequest.com/see5-info.html</u>
 
19
Schirmer T. and Cowan S., Prediction of membrane-spanning β-strands and its application to maltoporin, Protein Science, 2, p. 1361--1363, 1993.
 
20
Schulz G., β-barrel membrane proteins, Curr. Opin. Struct. Biology, 10, p. 443--447, 2000.
 
21
 
22
Vert J.-P., Support vector machine prediction of signal peptide cleavage site using a new class of kernels for strings, Proceedings of the Pacific Symposium on Biocomputing, p. 649--660, 2002.
23
24
 
25
Wimley W., Toward genomic identification of β-barrel membrane proteins: Composition and architecture of known structures, Protein Science, 11, p. 301--312, 2002.
 
26
 
27
Yuan Z., Prediction of protein subcellular locations using Markov chain models, FEBS Lett., 451, p. 23--26, 1999.
 
28
Zhai Y. and Saier M., The β-barrel finder (BBF) program, allowing identification of outer membrane β-barrel proteins encoded within prokaryotic genomes, Protein Science, 11, p. 2196--2207, 2002.


Collaborative Colleagues:
Rong She: colleagues
Fei Chen: colleagues
Ke Wang: colleagues
Martin Ester: colleagues
Jennifer L. Gardy: colleagues
Fiona S. L. Brinkman: colleagues