21 research outputs found
A Chaperonin Subunit with Unique Structures Is Essential for Folding of a Specific Substrate
Type I chaperonins are large, double-ring complexes present in bacteria (GroEL),
mitochondria (Hsp60), and chloroplasts (Cpn60), which are involved in mediating
the folding of newly synthesized, translocated, or stress-denatured proteins. In
Escherichia coli, GroEL comprises 14 identical subunits and
has been exquisitely optimized to fold its broad range of substrates. However,
multiple Cpn60 subunits with different expression profiles have evolved in
chloroplasts. Here, we show that, in Arabidopsis thaliana, the
minor subunit Cpn60β4 forms a heterooligomeric Cpn60 complex with
Cpn60α1 and Cpn60β1–β3 and is specifically required for the
folding of NdhH, a subunit of the chloroplast NADH dehydrogenase-like complex
(NDH). Other Cpn60β subunits cannot complement the function of Cpn60β4.
Furthermore, the unique C-terminus of Cpn60β4 is required for the full
activity of the unique Cpn60 complex containing Cpn60β4 for folding of NdhH.
Our findings suggest that this unusual kind of subunit enables the Cpn60 complex
to assist the folding of some particular substrates, whereas other dominant
Cpn60 subunits maintain a housekeeping chaperonin function by facilitating the
folding of other obligate substrates