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.
FEBS Lett
; 579(5): 1183-6, 2005 Feb 14.
Article
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| MEDLINE
| ID: mdl-15710410
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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Banco de datos:
MEDLINE
Asunto principal:
Rhodospirillum rubrum
/
Ribulosa-Bifosfato Carboxilasa
/
Tritio
/
Adenosina Trifosfato
/
Pliegue de Proteína
/
Chaperonina 60
/
Chaperonina 10
Idioma:
En
Año:
2005
Tipo del documento:
Article