Investigating protein domain combinations in complete proteomes.
Protein-related information is more accumulated rather than reduced to a synthetic view. Itemising properties of protein sequences is informative, so is the list of ingredients to do some cooking, but without a recipe, that is, quantification and chronology, understanding is incomplete. If the goal of accumulating information is to discover or reveal the function and related biochemical mechanisms, information has to be weighed and ordered. As a guideline, the weight of a piece of information should reflect how often it consistently occurs in various contexts. We propose a common sense approach to quantify and put data and information into perspective. Complete bacterial proteomes are individually mapped with the Pfam-A database of domains and protein family signatures in an attempt to assess the modularity of proteins at the level of a single proteome and the implications of a modular description of proteins for a functional interpretation. Poorly annotated proteins in the most documented bacteria (E. coli and B. subtilis) were considered in an attempt to formulate hypothesis on the basis of domain/module content.
Nikitin
Frédéric
F
Geneva Bioinformatics, Geneva 1206, Switzerland.
Lisacek
Frédérique
F
D001412:Bacillus subtilis / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D030562:Databases, Protein; D004926:Escherichia coli / Q000235:genetics; D016680:Genome, Bacterial; D020543:Proteome / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D020543:Proteome