PMID:10931176
| Citation |
Galat, A (2000) Sequence diversification of the FK506-binding proteins in several different genomes. Eur. J. Biochem. 267:4945-59 |
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| Abstract |
Sequences of FK506-binding proteins (FKBPs) from four genomes of the following organisms were compared: the prokaryote Escherichia coli, the lower eukaryote Saccharomyces cerevisiae, the plant Arabidopsis thaliana, the nematode Caenorhabditis elegans and a composite of 14 unique FKBPs from two mammalian organisms Homo sapiens (man) and Mus musculus (domestic mouse). A singular FK506-like binding domain (FKBD) has about 12 kDa and occurs in the form of archetypal FKBP-12 and as a part of different proteins ranging in size from 13 to 135 kDa. Some organisms may contain a variable number of proteins which consist from two to four consecutively fused FKBDs. In the 12-kDa subgroup of archetypal FKBPs sequence identity (ID) varies from 100 to 83% (mammalian FKBPs-12), 75-50% in mammalian vs. invertebrate FKBPs-12, and fall to about 30% for pairwise sequence comparisons of mammalian and bacterial FKBPs-12 which suggests that their sequences are divergent. Multiple sequence alignment of FKBPs from the four genomes and a set of unique mammalian FKBPs does not contain any explicit consensus sequence but certain sequence positions have conserved physico-chemical characteristics. Variations of hydrophobicity and bulkiness in the multiple sequence alignment are nonsymmetrical because the physico-chemical properties of the aligned sequences changed during evolution. These variations at the sequence positions which are crucial for binding the immunosuppressive macrolide FK506 and peptidyl-prolyl cis/trans isomerase (PPIase) activity are small. |
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| Keywords |
Amino Acid Sequence; Animals; Arabidopsis/genetics; Caenorhabditis elegans/genetics; Computer Graphics; Databases, Factual; Escherichia coli/genetics; Humans; Immunophilins/chemistry; Immunophilins/genetics; Mice; Models, Molecular; Molecular Sequence Data; Peptidylprolyl Isomerase/chemistry; Peptidylprolyl Isomerase/genetics; Protein Structure, Secondary; Saccharomyces cerevisiae/genetics; Sequence Alignment; Sequence Homology, Amino Acid; Tacrolimus Binding Proteins |
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