DnaJ (Hsp40) Homolog, Subfamily C, Member 24, also known as DNAJC24, is a member of the DnaJ/Hsp40 family of proteins. This family is known for its role in protein folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70-type chaperones . DNAJC24 is a protein-coding gene that plays a crucial role in various cellular processes.
The DNAJC24 gene is located on chromosome 11 and encodes a protein that contains a highly conserved J domain, which is characteristic of the DnaJ/Hsp40 family . This domain is essential for binding to Hsp70 chaperones and enhancing their ATPase activity. The protein also has iron-binding capabilities, which enhance its function as an electron carrier .
DNAJC24 is involved in the biosynthesis of diphthamide, a unique post-translationally modified histidine found in translation elongation factor-2 (EEF2) . This modification is conserved across species and serves as a target for ADP-ribosylation and inactivation by diphtheria toxin and Pseudomonas exotoxin A . The iron-bound form of DNAJC24 is redox-active and can function as an electron carrier, further enhancing its role in cellular processes .
Mutations or dysregulation of DNAJC24 have been linked to various diseases, including diphtheria and Joubert Syndrome 4 . Understanding the function and regulation of DNAJC24 can provide insights into the mechanisms underlying these diseases and potentially lead to the development of targeted therapies.
The recombinant form of DNAJC24 is produced using recombinant DNA technology, which involves inserting the DNAJC24 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein can be used for various research and therapeutic purposes, including studying its function, interactions, and potential as a drug target.