Does a bacterial elongation factor share a common evolutionary ancestor with actin?
Protein synthesis elongation factor Tu from E. coli shares several physical, chemical, and functional properties with actin-like proteins. Limited tryptic degradation indicates that the two polypeptides have a similar molecular architecture. These observations suggest that they could have evolved from a common ancestor, although more information will be necessary to prove or disprove this hypothesis. A partial sequence, comprising 22 aminoacid residues from the aminoterminal end of the large tryptic fragment of elongation factor Tu is presented.
D000199:Actins / Q000276:immunology; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins; D005075:Biological Evolution; D000939:Epitopes; D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology; D006868:Hydrolysis; D008565:Membrane Proteins; D008970:Molecular Weight; D010445:Peptide Elongation Factors; D011487:Protein Conformation; D012995:Solubility; D013329:Structure-Activity Relationship
D000199:Actins; D000596:Amino Acids; D001426:Bacterial Proteins; D000939:Epitopes; D008565:Membrane Proteins; D010445:Peptide Elongation Factors