Expansion and compression of a protein folding intermediate by GroEL. Academic Article

abstract

• The GroEL-GroES chaperonin system is required for the assisted folding of many essential proteins. The precise nature of this assistance remains unclear, however. Here we show that denatured RuBisCO from Rhodospirillum rubrum populates a stable, nonaggregating, and kinetically trapped monomeric state at low temperature. Productive folding of this nonnative intermediate is fully dependent on GroEL, GroES, and ATP. Reactivation of the trapped RuBisCO monomer proceeds through a series of GroEL-induced structural rearrangements, as judged by resonance energy transfer measurements between the amino- and carboxy-terminal domains of RuBisCO. A general mechanism used by GroEL to push large, recalcitrant proteins like RuBisCO toward their native states thus appears to involve two steps: partial unfolding or rearrangement of a nonnative protein upon capture by a GroEL ring, followed by spatial constriction within the GroEL-GroES cavity that favors or enforces compact, folding-competent intermediate states.

authors

• Rye, Hays

published proceedings

• Mol Cell

author list (cited authors)

• Lin, Z., & Rye, H. S.

citation count

• 78

complete list of authors

• Lin, Zong||Rye, Hays S

publication date

• January 2004

publisher

• Elsevier  Publisher

published in

• Molecular Cell  Journal

keywords

• Adenosine Triphosphate
• Chaperonin 10
• Chaperonin 60
• Kinetics
• Protein Folding
• Protein Structure, Tertiary
• Rhodospirillum Rubrum
• Ribulose-Bisphosphate Carboxylase
• Temperature
• Time Factors

Digital Object Identifier (DOI)

• 10.1016/j.molcel.2004.09.003

start page

• 23

end page

• 34

volume

• 16

issue

• 1

URL

• http://dx.doi.org/10.1016/j.molcel.2004.09.003