Can Hsp70 proteins act as force-generating motors?
Article Abstract:
The 70 kDa heat shock proteins that are molecular chaperones having an N- and C-terminal domain structure function as force-generating motors. Mitochondrial Hsp70 (mHsp70) species of the endoplasmic reticulum of yeast, undergo cross-linking to participate in protein translation by binding to a precursor chain. Lumenal Hsp70 accelerates the usually slow protein unfolding to a higher rate by inducing a pulling force on the precursor chain. Experiments demonstrate that lumenal Hsp70 binds to the membrane and display conformational modifications during ATP hydrolysis cycle while biochemical and genetic data indicate the requirement of the mHsp70-ISP45 interaction for protein translocation.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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A mammalian organelle map by protein correlation profiling
Article Abstract:
Integration of proteomic and genomic data enabled to identify networks of coexpressed genes, cis-regulatory motifs, and putative transcriptional regulators involved in organelle biogenesis. The analysis ties biochemistry, cell biology, and genomics into a common framework for organelle analysis.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
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The mechanisms of vesicle budding and fusion
Article Abstract:
The molecular mechanisms involved in selective cargo transport between organelles are studied. The transport by vesicular intermediates that bud from a donor compartment and fuse with an acceptor compartment is discussed.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2004
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