Högskolan i Skövde

his.sePublications
Planned maintenance
A system upgrade is planned for 10/12-2024, at 12:00-13:00. During this time DiVA will be unavailable.
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • apa-cv
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
In vivo characterization of Hsp104 variants in Saccharomyces cerevisiae
University of Skövde, School of Bioscience.
2021 (English)Independent thesis Advanced level (degree of Master (One Year)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

Cell stress, caused by misfolded or aggregated proteins or exposure to certain environmental stressors, activates stress detectors and selected analysis processes within the cell, resulting intranscriptional regulation and synthesis of factors that influence appropriate folding or removal of misaligned proteins to recover proteostasis. Yeasts are given a sophisticated and interconnected system to restore from the disruption of proteostasis, which involves molecular chaperones and protein degradation pathways as significant participants. Hsp104 is a stress response protein that, through an unknown mechanism, stimulates the reactivation of heatdamaged proteins in yeast. The aim of this thesis study is to learn more about Hsp104 function and location in young and old yeast cells. On the one hand, we aim to see how Hsp104 wildtype vs. mutant forms are distributed in young vs. elderly yeast cells. As a negative control, we employed the mutant variant of this protein. We also wanted to stress Hsp104 wildtype and mutant versions to see whether there are any variations in behaviour or protein levels. All research was carried out in yeast, with biochemical tests and high-throughput technologies like flow cytometry. Hsp104GFP signal were increased in the nucleus of Hsp104 wildtype cells with the increasing of cellular age. As well as, after heatshock treatment the Hsp104GFP aggregation was raised in Hsp104 wildtype and mutant forms. The results data demonstrated that Hsp104 protein levels were increased with cellular age and heatshock treatment enhanced the Hsp104 aggregation in Hsp104 wildtype and mutant forms.

Place, publisher, year, edition, pages
2021. , p. 21
National Category
Medical Bioscience
Identifiers
URN: urn:nbn:se:his:diva-20187OAI: oai:DiVA.org:his-20187DiVA, id: diva2:1577569
Subject / course
Bioscience
Supervisors
Examiners
Available from: 2021-07-02 Created: 2021-07-02 Last updated: 2021-07-02Bibliographically approved

Open Access in DiVA

fulltext(2268 kB)204 downloads
File information
File name FULLTEXT01.pdfFile size 2268 kBChecksum SHA-512
e82f6436fb2d5ebb9345afd68c79e4c5e43d2274968ed87b0033362b20cc27f5e91387b7943f531bcac0438a9fcbc775e3fe1ad8a6d4597d3aec80792259805f
Type fulltextMimetype application/pdf

By organisation
School of Bioscience
Medical Bioscience

Search outside of DiVA

GoogleGoogle Scholar
Total: 204 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

urn-nbn

Altmetric score

urn-nbn
Total: 453 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • apa-cv
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf