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Predicting secretory protein signal sequence cleavage sites by fusing the marks of global alignments

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Summary.

A newly synthesized secretory protein in cells bears a special sequence, called signal peptide or sequence, which plays the role of “address tag” in guiding the protein to wherever it is needed. Such a unique function of signal sequences has stimulated novel strategies for drug design or reprogramming cells for gene therapy. To realize these new ideas and plans, however, it is important to develop an automated method for fast and accurately identifying the signal sequences or their cleavage sites. In this paper, a new method is developed for predicting the signal sequence of a query secretory protein by fusing the results from a series of global alignments through a voting system. The very high success rates thus obtained suggest that the novel approach is very promising, and that the new method may become a useful vehicle in identifying signal sequence, or at least serve as a complementary tool to the existing algorithms of this field.

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Authors and Affiliations

  1. Institute of Image Processing and Pattern Recognition, Shanghai Jiaotong University, Shanghai, China

    D.-Q. Liu, H. Liu, H.-B. Shen, J. Yang & K.-C. Chou

  2. Gordon Life Science Institute, San Diego, CA, USA

    K.-C. Chou

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  1. D.-Q. Liu
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  2. H. Liu
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  3. H.-B. Shen
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  4. J. Yang
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Liu, DQ., Liu, H., Shen, HB. et al. Predicting secretory protein signal sequence cleavage sites by fusing the marks of global alignments. Amino Acids 32, 493–496 (2007). https://doi.org/10.1007/s00726-006-0466-z

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  • DOI: https://doi.org/10.1007/s00726-006-0466-z

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