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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Park ES,Fenton WA,Horwich ALdoi
10.1016/j.febslet.2005.01.013keywords:
subject
Has Abstractpub_date
2005-02-14 00:00:00pages
1183-6issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(05)00076-1journal_volume
579pub_type
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