Abstract
During evolution C-terminal peptide extensions were added to proteins on the gene level. These convey additional functions such as interaction with partner proteins or oligomerisation. IgM antibodies and molecular chaperones are two prominent examples discussed.
Highlights
Proteins are known as chains of amino acids which fold into well‐ defined three‐dimensional structures
The range of structural elements present in proteins is further expanded by N‐ terminal signal sequences of 30 to 50 residues needed for targeting to mitochondria and the endoplasmic reticulum (ER) that are cleaved after translocation across the membrane.[4]
The examples discussed in this review establish that nature evolved protein tags as independent functional units that can be added to the C‐terminal ends of proteins to foster protein interactions
Summary
The protein universe as we know is composed of folded structures and intrinsic disordered regions The latter may adopt structures upon interaction with binding partners. Some proteins contain C‐terminal extensions which act as independent functional units in the context of the protein. Since their activity does not depend on the protein context they can be considered as peptides in proteins. To illustrate this principle, we here discuss the C‐terminal extensions of IgM antibodies which dictate their assembly and the molecular chaperones Hsp[90], Hsp[70], and Hsp[104] which use C‐terminal peptide extensions as a docking site for interaction with different co‐chaperones.
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