1H, 15N and 13C resonance assignments of the J-domain of co-chaperone Sis1 from Saccharomyces cerevisiae

• Published in: Biomolecular NMR assignments 2018-10, Vol.12 (2), p.279-281
• Main Authors: Pinheiro, Glaucia M. S., Amorim, Gisele C., Iqbal, Anwar, Ramos, C. H. I., Almeida, Fabio C. L.
• Format: Article
• Language: English
• Subjects: Adenosine triphosphatase; Biochemistry; Biological and Medical Physics; Biophysics; Chaperones; Heat shock proteins; Hsp40 protein; Hsp70 protein; Physics; Physics and Astronomy; Polymer Sciences; Protein folding; Protein structure; Proteins; Resonance; Saccharomyces cerevisiae; Secondary structure; Translocation; Yeast
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-018-9823-6

Protein folding in the cell is usually aided by molecular chaperones, from which the Hsp70 (Hsp = heat shock protein) family has many important roles, such as aiding nascent folding and participating in translocation. Hsp70 has ATPase activity which is stimulated by binding to the J-domain present in co-chaperones from the Hsp40 family. Hsp40s have many functions, as for instance the binding to partially folded proteins to be delivered to Hsp70. However, the presence of the J-domain characterizes Hsp40s or, by this reason, as J-proteins. The J-domain alone can stimulate Hsp70 ATPase activity. Apparently, it also maintains the same conformation as in the whole protein although structural information on full J-proteins is still missing. This work reports the 1 H, 15 N and 13 C resonance assignments of the J-domain of a Hsp40 from Saccharomyces cerevisiae , named Sis1. Secondary structure and order parameter prediction from chemical shifts are also reported. Altogether, the data show that Sis1 J-domain is highly structured and predominantly formed by α-helices, results that are in very good agreement with those previously reported for the crystallographic structure.