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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Park ES,Fenton WA,Horwich AL

doi

10.1016/j.febslet.2005.01.013

keywords:

subject

Has Abstract

pub_date

2005-02-14 00:00:00

pages

1183-6

issue

5

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00076-1

journal_volume

579

pub_type

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