Abstract:
:Incubation of rhodanese with hche aperonins GroEL and GroES (1:2 GroEL14:GroES7 molar ratio) under functional and steady state conditions for ATP leads to the formation of a high proportion of rhodanese-bound symmetric complexes (GroEL14(GroES7)2), as revealed by native electrophoresis. Aliquots of such samples were observed under the electron microscope, and the symmetric particles were classified using neuronal networks and multivariate statistical analysis. Three different populations of symmetric particles were obtained which contained substrate in none, one or both GroEL cavities, respectively. The presence of substrate in the symmetric complexes under functional conditions supports their role as active intermediates in the protein folding cycle. These results also suggest that symmetric GroEL-GroES complexes can use both rings simultaneously for folding, probably increasing the efficiency of the reaction.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Llorca O,Marco S,Carrascosa JL,Valpuesta JMdoi
10.1016/s0014-5793(97)00186-5subject
Has Abstractpub_date
1997-03-24 00:00:00pages
195-9issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00186-5journal_volume
405pub_type
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