No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange
- PMID: 15710410
- DOI: 10.1016/j.febslet.2005.01.013
No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange
Abstract
In tritium-hydrogen exchange experiments, the large GroEL substrate Rubisco was unfolded and exchanged in urea/acid/tritiated water, then diluted into either protic buffer or protic buffer containing GroEL. The respective Rubisco metastable folding intermediate or Rubisco-GroEL binary complex was then separated from residual tritium after varying times of exchange by centrifugation through P-10 or G-25 resin. No significant tritium was recovered in either case, in contrast to an earlier report. Thus, although the earlier-proposed forced unfolding mechanism for the action of GroEL on a bound polypeptide, occurring during ATP/GroES binding, remains an attractive hypothesis, the data here do not provide any indication that it is involved in the folding of Rubisco.
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