scholarly journals Isolation of Physiologically Active Thylakoids and Their Use in Energy-Dependent Protein Transport Assays

10.3791/58393 ◽  
2018 ◽  
Author(s):  
Anthony Asher ◽  
Iniyan Ganesan ◽  
Laura Klasek ◽  
Steven M. Theg
Keyword(s):  
Protein Transport ◽  
Dependent Protein ◽  
Energy Dependent

scholarly journals Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex

2002 ◽  
Vol 157 (1) ◽  
pp. 63-78 ◽  
Author(s):  
Xinmin Li ◽  
Marcos P. Rivas ◽  
Min Fang ◽  
Jennifer Marchena ◽  
Bharat Mehrotra ◽  
...  
Keyword(s):  
Golgi Complex ◽  
Protein Transport ◽  
Adenosine Diphosphate ◽  
Functional Activities ◽  
Oxysterol Binding Protein ◽  
Golgi Region ◽  
Peripheral Membrane Protein ◽  
Dependent Protein ◽  
Altered Regulation

Oxysterol binding proteins (OSBPs) comprise a large conserved family of proteins in eukaryotes. Their ubiquity notwithstanding, the functional activities of these proteins remain unknown. Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p. We now demonstrate that Kes1p is a peripheral membrane protein of the yeast Golgi complex, that localization to the Golgi complex is required for Kes1p function in vivo, and that targeting of Kes1p to the Golgi complex requires binding to a phosphoinositide pool generated via the action of the Pik1p, but not the Stt4p, PtdIns 4-kinase. Localization of Kes1p to yeast Golgi region also requires function of a conserved motif found in all members of the OSBP family. Finally, we present evidence to suggest that Kes1p may regulate adenosine diphosphate-ribosylation factor (ARF) function in yeast, and that it may be through altered regulation of ARF that Kes1p interfaces with Sec14p in controlling Golgi region secretory function.

Intracellular regulation of protein degradation during sepsis is different in fast- and slow-twitch muscle

1997 ◽  
Vol 272 (3) ◽  
pp. R849-R856 ◽  
Author(s):  
G. Tiao ◽  
M. Lieberman ◽  
J. E. Fischer ◽  
P. O. Hasselgren
Keyword(s):  
Mrna Levels ◽  
Protein Breakdown ◽  
Ubiquitin Pathway ◽  
Differential Activation ◽  
Tissue Specific ◽  
Proteolytic Pathway ◽  
Dependent Protein ◽  
Slow Twitch ◽  
The Difference ◽  
Energy Dependent

We tested the hypothesis that the difference in the response to sepsis of protein breakdown between fast- and slow-twitch skeletal muscle reflects differential activation of the energy-ubiquitin-dependent proteolytic pathway. In addition, we defined the time course and the tissue specificity of sepsis-induced changes in the expression of the ubiquitin pathway. Sepsis was induced in rats by cecal ligation and puncture; control rats were sham operated. Energy-dependent protein breakdown was measured in incubated extensor digitorum longus (EDL) and soleus muscles. Ubiquitin mRNA levels were determined by Northern blot analysis. Sepsis resulted in increased energy-dependent protein breakdown and upregulated expression of ubiquitin mRNA in the fast-twitch EDL but not in the slow-twitch soleus muscle. The sepsis-induced increase in ubiquitin mRNA levels in the EDL muscle was noticeable before the increase in energy-dependent protein breakdown. Sepsis increased ubiquitin mRNA levels in the diaphragm (a mixed fiber-type muscle) but not in heart, liver, kidney, or intestine, consistent with a tissue-specific regulation of the ubiquitin system during sepsis. The results suggest that the difference in protein breakdown during sepsis between fast- and slow-twitch muscles reflects differential activation of the energy-ubiquitin-dependent proteolytic pathway. The data also suggest that the expression of the ubiquitin pathway is upregulated in a time-dependent fashion during sepsis and that this response is not a generalized phenomenon but is tissue specific.

scholarly journals The Arabidopsispex12andpex13mutants are defective in both PTS1- and PTS2-dependent protein transport to peroxisomes

2006 ◽  
Vol 47 (4) ◽  
pp. 604-618 ◽  
Author(s):  
Shoji Mano ◽  
Chihiro Nakamori ◽  
Kazumasa Nito ◽  
Maki Kondo ◽  
Mikio Nishimura
Keyword(s):  
Protein Transport ◽  
Dependent Protein

scholarly journals Enough is enough: TatA demand during Tat-dependent protein transport

2013 ◽  
Vol 1833 (5) ◽  
pp. 957-965 ◽  
Author(s):  
René Steffen Hauer ◽  
René Schlesier ◽  
Kathleen Heilmann ◽  
Julia Dittmar ◽  
Mario Jakob ◽  
...  
Keyword(s):  
Protein Transport ◽  
Dependent Protein

scholarly journals Chloroplast TatC plays a direct role in thylakoid ΔpH-dependent protein transport

FEBS Letters ◽  
2001 ◽  
Vol 501 (1) ◽  
pp. 65-68 ◽  
Author(s):  
Hiroki Mori ◽  
Elizabeth J. Summer ◽  
Kenneth Cline
Keyword(s):  
Protein Transport ◽  
Direct Role ◽  
Dependent Protein

scholarly journals Component Specificity for the Thylakoidal Sec and Delta Ph–Dependent Protein Transport Pathways

1999 ◽  
Vol 146 (1) ◽  
pp. 45-56 ◽  
Author(s):  
Hiroki Mori ◽  
Elizabeth J. Summer ◽  
Xianyue Ma ◽  
Kenneth Cline
Keyword(s):  
Protein Transport ◽  
Signal Recognition Particle ◽  
Thylakoid Membranes ◽  
Transport Pathways ◽  
Sec Pathway ◽  
Evolutionarily Conserved ◽  
In Series ◽  
Dependent Protein ◽  
Membrane Components ◽  
Substrate Proteins

Prokaryotes and prokaryote-derived thylakoid membranes of chloroplasts share multiple, evolutionarily conserved pathways for protein export. These include the Sec, signal recognition particle (SRP), and Delta pH/Tat systems. Little is known regarding the thylakoid membrane components involved in these pathways. We isolated a cDNA clone to a novel component of the Delta pH pathway, Tha4, and prepared antibodies against pea Tha4, against maize Hcf106, a protein implicated in Delta pH pathway transport by genetic studies, and against cpSecY, the thylakoid homologue of the bacterial SecY translocon protein. These components were localized to the nonappressed thylakoid membranes. Tha4 and Hcf106 were present in ∼10-fold excess over active translocation sites. Antibodies to either Tha4 or Hcf106 inhibited translocation of four known Delta pH pathway substrate proteins, but not of Sec pathway or SRP pathway substrates. This suggests that Tha4 and Hcf106 operate either in series or as subunits of a heteromultimeric complex. cpSecY antibodies inhibited translocation of Sec pathway substrates but not of Delta pH or SRP pathway substrates. These studies provide the first biochemical evidence that Tha4 and Hcf106 are specific components of the Delta pH pathway and provide one line of evidence that cpSecY is used specifically by the Sec pathway.

Activity Dependent Protein Transport from the Synapse to the Nucleus

Dendrites ◽  
2016 ◽  
pp. 111-124
Author(s):  
Sujoy Bera ◽  
Gonca Bayraktar ◽  
Katarzyna M. Grochowska ◽  
Michelle Melgarejo da Rosa ◽  
Michael R. Kreutz
Keyword(s):  
Protein Transport ◽  
Dependent Protein ◽  
Activity Dependent
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