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Full-Text Articles in Other Biochemistry, Biophysics, and Structural Biology
The Identity Of Proteins Associated With A Small Heat Shock Protein During Heat Stress In Vivo Indicates That These Chaperones Protect A Wide Range Of Cellular Functions, Eman Basha, Garrett J. Lee, Linda A. Breci, Andrew C. Hausrath, Nicole R. Buan, Kim C. Giese, Elizabeth Vierling
The Identity Of Proteins Associated With A Small Heat Shock Protein During Heat Stress In Vivo Indicates That These Chaperones Protect A Wide Range Of Cellular Functions, Eman Basha, Garrett J. Lee, Linda A. Breci, Andrew C. Hausrath, Nicole R. Buan, Kim C. Giese, Elizabeth Vierling
Department of Biochemistry: Faculty Publications
The small heat shock proteins (sHSPs) are a ubiquitous class of ATP-independent chaperones believed to prevent irreversible protein aggregation and to facilitate subsequent protein renaturation in cooperation with ATP-dependent chaperones. Although sHSP chaperone activity has been studied extensively in vitro, understanding the mechanism of sHSP function requires identification of proteins that are sHSP substrates in vivo. We have used both immunoprecipitation and affinity chromatography to recover 42 proteins that specifically interact with Synechocystis Hsp16.6 in vivo during heat treatment. These proteins can all be released from Hsp16.6 by the ATP-dependent activity of DnaK and cochaperones and are heat-labile. Thirteen …
5-Hydroxydecanoate Is Metabolised In Mitochondria And Creates A Rate-Limiting Bottleneck For Β-Oxidation Of Fatty Acids, Peter J. Hanley, Stefan Dröse, Ulrich Brandt, Rachel A. Lareau, Abir L. Banerjee, D. K. Srivastava, Leonard J. Banaszak, Joseph J. Barycki, Paul P. Van Veldhoven, Jürgen Daut
5-Hydroxydecanoate Is Metabolised In Mitochondria And Creates A Rate-Limiting Bottleneck For Β-Oxidation Of Fatty Acids, Peter J. Hanley, Stefan Dröse, Ulrich Brandt, Rachel A. Lareau, Abir L. Banerjee, D. K. Srivastava, Leonard J. Banaszak, Joseph J. Barycki, Paul P. Van Veldhoven, Jürgen Daut
Department of Biochemistry: Faculty Publications
5-Hydroxydecanoate (5-HD) blocks pharmacological and ischaemic preconditioning, and
has been postulated to be a specific inhibitor of mitochondrial ATP-sensitive K+ (KATP)
channels. However, recent work has shown that 5-HD is activated to 5-hydroxydecanoyl-CoA
(5-HD-CoA), which is a substrate for the first step of β-oxidation. We have now
analysed the complete β-oxidation of 5-HD-CoA using specially synthesised (and purified)
substrates and enzymes, as well as isolated rat liver and heart mitochondria, and compared
it with the metabolism of the physiological substrate decanoyl-CoA. At the second step of
β-oxidation, catalysed by enoyl-CoA hydratase, enzyme kinetics were …
Interactions Between Small Heat Shock Protein Subunits And Substrate In Small Heat Shock Protein-Substrate Complexes, Kenneth L. Friedrich, Kim C. Giese, Nicole R. Baun, Elizabeth Vierling
Interactions Between Small Heat Shock Protein Subunits And Substrate In Small Heat Shock Protein-Substrate Complexes, Kenneth L. Friedrich, Kim C. Giese, Nicole R. Baun, Elizabeth Vierling
Department of Biochemistry: Faculty Publications
Small heat shock proteins (sHSPs) are dynamic oligomeric
proteins that bind unfolding proteins and protect
them from irreversible aggregation. This binding results
in the formation of sHSP-substrate complexes from
which substrate can later be refolded. Interactions between
sHSP and substrate in sHSP-substrate complexes
and the mechanism by which substrate is transferred to
ATP-dependent chaperones for refolding are poorly defined.
We have established C-terminal affinity-tagged
sHSPs from a eukaryote (pea HSP18.1) and a prokaryote
(Synechocystis HSP16.6) as tools to investigate these issues.
We demonstrate that sHSP subunit exchange for
HSP18.1 and HSP16.6 is temperature-dependent and
rapid at the optimal growth …
Interactions Between Small Heat Shock Protein Subunits And Substrate In Small Heat Shock Protein-Substrate Complexes, Kenneth L. Friedrich,, Kim C. Giese, Nicole R. Buan, Elizabeth Vierling
Interactions Between Small Heat Shock Protein Subunits And Substrate In Small Heat Shock Protein-Substrate Complexes, Kenneth L. Friedrich,, Kim C. Giese, Nicole R. Buan, Elizabeth Vierling
Department of Biochemistry: Faculty Publications
Small heat shock proteins (sHSPs) are dynamic oligomeric proteins that bind unfolding proteins and protect them from irreversible aggregation. This binding results in the formation of sHSP-substrate complexes from which substrate can later be refolded. Interactions between sHSP and substrate in sHSP-substrate complexes and the mechanism by which substrate is transferred to ATP-dependent chaperones for refolding are poorly defined. We have established C-terminal affinity-tagged sHSPs from a eukaryote (pea HSP18.1) and a prokaryote (Synechocystis HSP16.6) as tools to investigate these issues. We demonstrate that sHSP subunit exchange for HSP18.1 and HSP16.6 is temperature-dependent and rapid at the optimal growth temperature …
Mobilization Of Intracellular Copper Stores By The Ctr2 Vacuolar Copper Transporter, Erin M. Rees, Jaekwon Lee, Dennis J. Thiele
Mobilization Of Intracellular Copper Stores By The Ctr2 Vacuolar Copper Transporter, Erin M. Rees, Jaekwon Lee, Dennis J. Thiele
Department of Biochemistry: Faculty Publications
Copper plays an essential role in processes including signaling to the transcription and protein trafficking machinery, oxidative phosphorylation, iron mobilization, neuropeptide maturation, and normal development. Whereas much is known about intracellular mobilization of ions such as calcium, little information is available on how eukaryotic cells mobilize intracellular copper stores. We describe a mechanism by which the Saccharomyces cerevisiae Ctr2 protein provides bioavailable copper via mobilization of intracellular copper stores. Whereas Ctr2 exhibits structural similarity to the Ctr1 plasma membrane copper importer, microscopic and biochemical fractionation studies localize Ctr2 to the vacuole membrane. We demonstrate that Ctr2 mobilizes vacuolar copper stores …
The Identity Of Proteins Associated With A Small Heat Shock Protein During Heat Stress In Vivo Indicates That These Chaperones Protect A Wide Range Of Cellular Functions, Eman Basha, Garrett J. Lee, Linda A. Breci, Andrew C. Hausrath, Nicole R. Baun, Kim C. Giese, Elizabeth Vierling
The Identity Of Proteins Associated With A Small Heat Shock Protein During Heat Stress In Vivo Indicates That These Chaperones Protect A Wide Range Of Cellular Functions, Eman Basha, Garrett J. Lee, Linda A. Breci, Andrew C. Hausrath, Nicole R. Baun, Kim C. Giese, Elizabeth Vierling
Department of Biochemistry: Faculty Publications
The small heat shock proteins (sHSPs) are a ubiquitous
class of ATP-independent chaperones believed to
prevent irreversible protein aggregation and to facilitate
subsequent protein renaturation in cooperation
with ATP-dependent chaperones. Although sHSP chaperone
activity has been studied extensively in vitro, understanding
the mechanism of sHSP function requires
identification of proteins that are sHSP substrates in
vivo. We have used both immunoprecipitation and affinity
chromatography to recover 42 proteins that specifically
interact with Synechocystis Hsp16.6 in vivo during
heat treatment. These proteins can all be released from
Hsp16.6 by the ATP-dependent activity of DnaK and cochaperones
and are heat-labile. …