首页    期刊浏览 2024年12月05日 星期四
登录注册

文章基本信息

  • 标题:Solute diffusion is hindered in the mitochondrial matrix
  • 本地全文:下载
  • 作者:Cindy E. J. Dieteren ; Stan C. A. M. Gielen ; Leo G. J. Nijtmans
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2011
  • 卷号:108
  • 期号:21
  • 页码:8657-8662
  • DOI:10.1073/pnas.1017581108
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Intracellular chemical reactions generally constitute reaction-diffusion systems located inside nanostructured compartments like the cytosol, nucleus, endoplasmic reticulum, Golgi, and mitochondrion. Understanding the properties of such systems requires quantitative information about solute diffusion. Here we present a novel approach that allows determination of the solvent-dependent solute diffusion constant (Dsolvent) inside cell compartments with an experimentally quantifiable nanostructure. In essence, our method consists of the matching of synthetic fluorescence recovery after photobleaching (FRAP) curves, generated by a mathematical model with a realistic nanostructure, and experimental FRAP data. As a proof of principle, we assessed Dsolvent of a monomeric fluorescent protein (AcGFP1) and its tandem fusion (AcGFP12) in the mitochondrial matrix of HEK293 cells. Our results demonstrate that diffusion of both proteins is substantially slowed by barriers in the mitochondrial matrix (cristae), suggesting that cells can control the dynamics of biochemical reactions in this compartment by modifying its nanostructure.
  • 关键词:molecular dynamics ; quantitative random-walk model ; systems biology
国家哲学社会科学文献中心版权所有