Name
Title | ||
|---|---|---|
Large-Scale Conformational Transitions And Dimerization Are Encoded In The Amino-Acid Sequences Of Hsp70 Chaperones |
Abstract | ||
|---|---|---|
Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteostasis in the cell. Hsp70s assist a myriad of cellular processes by binding unfolded or misfolded substrates during a complex biochemical cycle involving large-scale structural rearrangements. Here we show that an analysis of coevolution at the residue level fully captures the characteristic large-scale conformational transitions of this protein family, and predicts an evolutionary conserved-and thus functional-homo-dimeric arrangement. Furthermore, we highlight that the features encoding the Hsp70 dimer are more conserved in bacterial than in eukaryotic sequences, suggesting that the known Hsp70/Hsp110 hetero-dimer is a eukaryotic specialization built on a preexisting template. |
Year | DOI | Venue |
|---|---|---|
2015 | 10.1371/journal.pcbi.1004262 | PLOS COMPUTATIONAL BIOLOGY |
Field | DocType | Volume |
Sequence alignment,Protein family,Protein structure prediction,Proteostasis,Biology,Amino acid,Fungal protein,Bioinformatics,Chaperone (protein),Genetics,Peptide sequence | Journal | 11 |
Issue | ISSN | Citations |
6 | 1553-734X | 4 |
PageRank | References | Authors |
0.41 | 4 | 4 |
Name | Order | Citations | PageRank |
|---|---|---|---|
| Duccio Malinverni | 1 | 4 | 0.41 |
| Simone Marsili | 2 | 12 | 1.69 |
| Alessandro Barducci | 3 | 33 | 5.60 |
| Paolo De Los Rios | 4 | 13 | 3.11 |