Chapter title |
Complementation Assays for Co-chaperone Function.
|
---|---|
Book title |
Chaperones
|
Published in |
Methods in molecular biology, January 2023
|
DOI | 10.1007/978-1-0716-3342-7_9 |
Pubmed ID | |
Book ISBNs |
978-1-07-163341-0, 978-1-07-163342-7
|
Authors |
Edkins, Adrienne L, Blatch, Gregory L, Adrienne L. Edkins, Gregory L. Blatch, Edkins, Adrienne L., Blatch, Gregory L. |
Abstract |
The development of mutant microorganisms lacking J domain proteins (JDPs; formerly called Hsp40s) has enabled the development of complementation assays for testing the co-chaperone function of JDPs. In these assays, an exogenously expressed novel JDP is tested for its ability to functionally substitute for a non-expressed or nonfunctional endogenous JDP(s) by reversing a stress phenotype. For example, the in vivo functionality of prokaryotic JDPs can be tested on the basis of their ability to reverse the thermosensitivity of a dnaJ cbpA mutant strain of the bacterium Escherichia coli (OD259). Similarly, the in vivo functionality of eukaryotic JDPs can be assessed in a thermosensitive ydj1 mutant strain of the yeast Saccharomyces cerevisiae (JJ160). Here we outline the use of these thermosensitive microorganisms in complementation assays to functionally characterize a JDP from the bacterium, Agrobacterium tumefaciens (AgtDnaJ), and a JDP from the trypanosomal parasite, Trypanosoma cruzi (TcJ2). |
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