Secreted protein and peptide biosynthesis: Precursor structures and processing mechanisms

Protein biosynthesis is rarely restricted to mRNA translation into an amino acid sequence. To yield the mature form, most proteins undergo various posttranslational modifications due to the action of different enzymes. Certain combinations of amino acid residues (primary structure motifs) have been defined to guide the sequence of modifications during the process of precursor protein maturation into the final product. In this chapter, we specifically focus on the secreted polypeptide maturation. For a number of precursor sequences retrieved from UniProt databank, complete sets of enzymes have been identified that execute processing of secreted polypeptides. This finds reflection in the amino acid sequences of the corresponding protein precursors that carry information about the queue of posttranslational events in the form of specific motifs arrangement. Extensive data analysis allowed us to propose a simple set of principals that facilitate effective sequence information handling. Utilization of the proposed principals significantly improves mature protein sequence prediction from available gene structures. We also address the problem of known motif identification and novel motif prediction from large sets of data. A number of proteins are considered in greater detail as examples of the proposed principals utilization conveniences. © 2009 by Nova Science Publishers, Inc. All rights reserved.

IBCH: 516
Кол-во цитирований на 12.2023: 10
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