Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.
Science
; 347(6229): 1485-9, 2015 Mar 27.
Article
em En
| MEDLINE
| ID: mdl-25814585
ABSTRACT
During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (α-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex for recycling of the SNARE proteins. The molecular mechanism by which NSF disassembles the SNARE complex is largely unknown. Using single-molecule fluorescence spectroscopy and magnetic tweezers, we found that NSF disassembled a single SNARE complex in only one round of adenosine triphosphate (ATP) turnover. Upon ATP cleavage, the NSF hexamer developed internal tension with dissociation of phosphate ions. After latent time measuring tens of seconds, NSF released the built-up tension in a burst within 20 milliseconds, resulting in disassembly followed by immediate release of the SNARE proteins. Thus, NSF appears to use a "spring-loaded" mechanism to couple ATP hydrolysis and unfolding of substrate proteins.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trifosfato de Adenosina
/
Proteínas Sensíveis a N-Etilmaleimida
/
Proteínas SNARE
/
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida
Limite:
Animals
Idioma:
En
Revista:
Science
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Coréia do Sul