scholarly journals Efficient Tor Signaling Requires a Functional Class C Vps Protein Complex inSaccharomyces cerevisiae

Genetics ◽  
2007 ◽  
Vol 176 (4) ◽  
pp. 2139-2150 ◽  
Author(s):  
Sara A. Zurita-Martinez ◽  
Rekha Puria ◽  
Xuewen Pan ◽  
Jef D. Boeke ◽  
Maria E. Cardenas
Keyword(s):  
Protein Complex ◽  
Functional Class ◽  
Tor Signaling ◽  
Class C

scholarly journals Class C Vps Protein Complex Regulates Vacuolar SNARE Pairing and Is Required for Vesicle Docking/Fusion

2000 ◽  
Vol 6 (3) ◽  
pp. 661-671 ◽  
Author(s):  
Trey K. Sato ◽  
Peter Rehling ◽  
Michael R. Peterson ◽  
Scott D. Emr
Keyword(s):  
Protein Complex ◽  
Vesicle Docking ◽  
Class C

scholarly journals Yeast homotypic vacuole fusion requires the Ccz1–Mon1 complex during the tethering/docking stage

2003 ◽  
Vol 163 (5) ◽  
pp. 973-985 ◽  
Author(s):  
Chao-Wen Wang ◽  
Per E. Stromhaug ◽  
Emily J. Kauffman ◽  
Lois S. Weisman ◽  
Daniel J. Klionsky
Keyword(s):  
Protein Complex ◽  
Complex Interaction ◽  
Snare Complex ◽  
Morphological Evidence ◽  
Vacuole Membrane ◽  
Vacuole Fusion ◽  
Class C ◽  
Hops Complex

The function of the yeast lysosome/vacuole is critically linked with the morphology of the organelle. Accordingly, highly regulated processes control vacuolar fission and fusion events. Analysis of homotypic vacuole fusion demonstrated that vacuoles from strains defective in the CCZ1 and MON1 genes could not fuse. Morphological evidence suggested that these mutant vacuoles could not proceed to the tethering/docking stage. Ccz1 and Mon1 form a stable protein complex that binds the vacuole membrane. In the absence of the Ccz1–Mon1 complex, the integrity of vacuole SNARE pairing and the unpaired SNARE class C Vps/HOPS complex interaction were both impaired. The Ccz1–Mon1 complex colocalized with other fusion components on the vacuole as part of the cis-SNARE complex, and the association of the Ccz1–Mon1 complex with the vacuole appeared to be regulated by the class C Vps/HOPS complex proteins. Accordingly, we propose that the Ccz1–Mon1 complex is critical for the Ypt7-dependent tethering/docking stage leading to the formation of a trans-SNARE complex and subsequent vacuole fusion.

Contribution of PO2, P50, and Hb to changes in arteriovenous O2 content during exercise in heart failure

1996 ◽  
Vol 80 (2) ◽  
pp. 623-631 ◽  
Author(s):  
G. B. Perego ◽  
G. C. Marenzi ◽  
M. Guazzi ◽  
P. Sganzerla ◽  
E. Assanelli ◽  
...  
Keyword(s):  
Heart Failure ◽  
Normal Subjects ◽  
Cardiopulmonary Exercise Test ◽  
Functional Class ◽  
Whole Body ◽  
Peak Exercise ◽  
Class A ◽  
Patients With Heart Failure ◽  
Concentration Changes ◽  
Class C

Arteriovenous O2 content (a-vCO2) differences increase during exercise in normal subjects through several mechanisms including PO2, O2 pressure at which hemoglobin (Hb) is half saturated with O2 (P50), and Hb concentration changes. The present study was undertaken to evaluate how much these biochemical changes are relevant to a-vCO2 difference through exercise in patients with heart failure. Twenty-seven patients with congestive heart failure [10 patients in functional class A (peak exercise O2 uptake =20 ml x kg-1 x min-1), 9 in class B (20-15 ml x kg-1 x min-1), and 8 in class C (15-10 ml x kg-1 x min-1)] underwent a cardiopulmonary exercise test with once-per-minute simultaneous blood sampling from the pulmonary and systemic arteries for determination of Hb, PO2, PCO2, pH, O2 content (CO2), Hb saturation and lactic acid (pulmonary artery only), and calculation of P50. Analysis of data was done at six exercise stages: the first at rest, the last at peak exercise, and the second to the fifth at one-, two-, three-, and four-fifths of O2 consumption increase. a-vCO2 difference at peak exercise was 14.3 +/- 2.1, 16.9 +/- 2.4, and 14.7 +/- 2.1 (SD) ml/dl in class A, B, and C patients, respectively. The contribution of Hb, P50, and PO2 changes to the increments of a-vCO2 difference during exercise was 21, 17, and 63%, respectively; the only interclass difference observed was for P50, which plays a greater role in a-vCO2 difference in class A. Hb changes act mainly at the arterial site, whereas P50 and PO2 act at the venous site. Hb increase was constant through the test, venous P50 increase was greater above anaerobic threshold, and venous PO2 reduction was most remarkable at the onset of exercise; in class C patients, no venous PO2 change was recorded in the second half of exercise. Thus a-vCO2 difference increase during exercise is notable in patients with heart failure but unrelated to the severity of the syndrome. Hb, P50, and, to the greatest degree, PO2 changes participate in the increment of a-vCO2 difference. In class C patients, the lack of PO2 reduction in the second half of exercise suggests the achievement of a “whole body critical venous PO2.”

scholarly journals A Novel RING Finger Protein Complex Essential for a Late Step in Protein Transport to the Yeast Vacuole

1997 ◽  
Vol 8 (11) ◽  
pp. 2307-2327 ◽  
Author(s):  
Stephanie E. Rieder ◽  
Scott D. Emr
Keyword(s):  
Protein Complex ◽  
Protein Transport ◽  
Protein Sorting ◽  
Ring Finger ◽  
Endocytic Pathway ◽  
Vacuolar Protein Sorting ◽  
Oligomeric Protein ◽  
Late Step ◽  
Class C ◽  
Vacuolar Protein

Protein transport to the lysosome-like vacuole in yeast is mediated by multiple pathways, including the biosynthetic routes for vacuolar hydrolases, the endocytic pathway, and autophagy. Among the more than 40 genes required for vacuolar protein sorting (VPS) inSaccharomyces cerevisiae, mutations in the four class CVPS genes result in the most severe vacuolar protein sorting and morphology defects. Herein, we provide complementary genetic and biochemical evidence that the class C VPSgene products (Vps18p, Vps11p, Vps16p, and Vps33p) physically and functionally interact to mediate a late step in protein transport to the vacuole. Chemical cross-linking experiments demonstrated that Vps11p and Vps18p, which both contain RING finger zinc-binding domains, are components of a hetero-oligomeric protein complex that includes Vps16p and the Sec1p homologue Vps33p. The class C Vps protein complex colocalized with vacuolar membranes and a distinct dense membrane fraction. Analysis of cells harboring a temperature-conditionalvps18 allele (vps18tsf) indicated that Vps18p function is required for the biosynthetic, endocytic, and autophagic protein transport pathways to the vacuole. In addition,vps18tsfcells accumulated multivesicular bodies, autophagosomes, and other membrane compartments that appear to represent blocked transport intermediates. Overproduction of either Vps16p or the vacuolar syntaxin homologue Vam3p suppressed defects associated with vps18tsfmutant cells, indicating that the class C Vps proteins and Vam3p may functionally interact. Thus we propose that the class C Vps proteins are components of a hetero-oligomeric protein complex that mediates the delivery of multiple transport intermediates to the vacuole.

High-Resolution electron crystallography of the light-harvesting chlorophyll-a/b protein complex from chloroplast membranes

1990 ◽  
Vol 48 (1) ◽  
pp. 610-610
Author(s):  
Werner Kühlbrandt ◽  
Da Neng Wang ◽  
K.H. Downing
Keyword(s):  
High Resolution ◽  
Electron Diffraction ◽  
Chlorophyll A ◽  
Protein Complex ◽  
Structural Integrity ◽  
Light Harvesting ◽  
Lhc Ii ◽  
Diffraction Patterns ◽  
Difference Fourier ◽  
2D Crystals

The light-harvesting chlorophyll-a/b protein complex (LHC-II) is the most abundant membrane protein in the chloroplasts of green plants where it functions as a molecular antenna of solar energy for photosynthesis. We have grown two-dimensional (2d) crystals of the purified, detergent-solubilized LHC-II . The crystals which measured 5 to 10 μm in diameter were stabilized for electron microscopy by washing with a 0.5% solution of tannin. Electron diffraction patterns of untilted 2d crystals cooled to 130 K showed sharp spots to 3.1 Å resolution. Spot-scan images of 2d crystals were recorded at 160 K with the Berkeley microscope . Images of untilted crystals were processed, using the unbending procedure by Henderson et al . A projection map of the complex at 3.7Å resolution was generated from electron diffraction amplitudes and high-resolution phases obtained by image processing .A difference Fourier analysis with the same image phases and electron diffraction amplitudes recorded of frozen, hydrated specimens showed no significant differences in the 3.7Å projection map. Our tannin treatment therefore does not affect the structural integrity of the complex.

Use of Antibody to aid Visualization of Protein at the Termini of Bacteriophage Ø29 DNA

1980 ◽  
Vol 38 ◽  
pp. 540-541
Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly
Keyword(s):  
Electron Microscopy ◽  
Bacillus Subtilis ◽  
Dna Synthesis ◽  
Restriction Endonuclease ◽  
Protein Complex ◽  
Protein Product ◽  
Viral Dna ◽  
Small Proteins ◽  
Antibody Labeling ◽  
Subtilis Bacteriophage

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.

118 NT-proBNP values and Weber functional class classification in patients with chronic heart failure

2007 ◽  
Vol 6 (1) ◽  
pp. 29-29
Author(s):  
R FERNANDES ◽  
R SOARES ◽  
J FELICIANO ◽  
J SERRA ◽  
A MAMEDE ◽  
...  
Keyword(s):  
Heart Failure ◽  
Chronic Heart Failure ◽  
Functional Class

235 E/Vp is related to the functional class in a population with dyspnea

2006 ◽  
Vol 5 (1) ◽  
pp. 47-48
Author(s):  
M RIVERAOTERO ◽  
L MAINAR ◽  
M SANCHOTELLO ◽  
E ROSELLO ◽  
V CLIMENT ◽  
...  
Keyword(s):  
Functional Class
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