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Table 1 Identification of yeast proteins involved in recombinant MuHN and MeH expression.

From: Overexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae

Spot No. Namea Fold Changeb ID Methodc Function, Processd Localization Fraction overexpressede
1,2
3
Ssa1/2
Ssa4
2.4 ± 0.2f M, ESI
ESI
Chaperone, Stress response
Chaperone, Stress response
Cytoplasm, cell wall
Cytoplasm, nucleus
All fractions except insoluble under denaturing conditions
All fractions except insoluble under denaturing conditions
4 Kar2 3.8 ± 0.4 M Chaperone, UPR Endoplasmic reticulum Soluble at high salt concentration
5 Sse1 2.3 ± 0.2 ESI Co-chaperone, Stress response Cytoplasm Soluble at high salt concentration
6 Hsc82 2.1 ± 0.3 M, ESI Chaperone, Stress response Cytoplasm, mitochondrion Soluble at high salt concentration
7 Eno2 1.5 ± 0.2 M Lyase, Glycolysis Cytoplasm, vacuole Totally soluble
8 Sgt2 1.6 ± 0.2 ESI Co-chaperone, Response to heat Cytoplasm Soluble in non-ionic detergent
9 Sti1 1.6 ± 0.3 M Co-chaperone, Stress response Cytoplasm Soluble at high salt concentration
10 Hsp104 2.6 ± 0.3 ESI Chaperone, Stress response Cytoplasm, nucleus Soluble at high salt concentration
11 Hsp26 0.7 ± 0.1 M Chaperone, Stress response Cytoplasm, nucleus Insoluble under native conditions
12 Hsp42 NDg M Chaperone, Stress response Cytoplasm, cytoskeleton Insoluble under native conditions
13 Bgl2 NDg M Glycosidase, cell wall organization Cell wall Insoluble under native conditions
14 Pep4 NDg M Protease, respon- se to starvation Vacuole, mitochondrion Insoluble under native conditions
15 Tef2 NAg ESI Elongation factor, Translation Cytoskeleton, Ribosome Insoluble under denaturing conditions
  1. aAccepted name from the Saccharomyces genome database (SGD) and YPD. Spots 1 and 2 represent mixtures of similar proteins Ssa1 and Ssa2 (97% identity) at an unknown ratio.
  2. bFold change represents ratio between the relative protein amounts (%Vol) in whole cell lysates of the MuHN/MeH expressing and control cells, respectively, ±SD.
  3. cProtein identification method abbreviations: M, MALDI-fingerprint; ESI, nLC-ESI-MS/MS analysis.
  4. dMolecular function, biological process and localization are noted according to UniProtKB and SGD.
  5. eLysates were fractionated into different fractions based on protein solubility under various conditions as described in Methods and shown in Figure 3. Fractions with the strongest overexpression of identified yeast proteins in MuHN and/or MeH variants compared to control samples are indicated.
  6. fThree closely packed spots 1, 2 and 3 were merged and the fold change calculated for one common Ssa spot.
  7. gND - not determined; NA - not assayed.