Čaperon Hsp90 – uloge u smatanju proteina i pokretanju noviteta u evoluciji

undergraduate thesis

• Title (english): Chaperone Hsp90 – Roles in Protein Folding and Establishment of Novelties in Evolution
• Author: Ana Verbanac
• Mentor: Marko Močibob (mentor)
• Granter: University of Zagreb; Faculty of Science; (Department of Biology); Zagreb
• Granter: University of Zagreb; Faculty of Science; (Department of Chemistry); Zagreb
• Defense date and country: 2022-09-21, Croatia
• Scientific / art field, discipline and subdiscipline: NATURAL SCIENCES; Biology

Abstract

Čaperon Hsp90 jedan je od ključnih regulatora proteostaze pod normalnim i stresnim uvjetima za
eukariotsku stanicu. Proteini iz obitelji Hsp90 pronađeni su u bakterijama, citosolu,
endoplazmatskom retikulumu, mitohondriju i kloroplastu. Svi homolozi imaju slične strukture i
funkcije zato što je riječ o vrlo konzerviranoj obitelji proteina. Sa svojim supstratima stvara
komplekse te omogućuje konformacijske rearanžmane i poprimanje aktivne strukture proteina
supstrata. Uz njih, bitnu ulogu imaju kočaperoni koji interagiraju sa čaperonom i reguliraju
ATPaznu aktivnost, konformacijski ciklus Hsp90 dimera i interakciju sa drugim čaperonima.
Hsp90 može imati i ulogu puferiranja i potenciranja genetičke varijacije i poticanja noviteta u
evoluciji. Razumijevanje dinamike Hsp90 i kočaperona omogućuje razumijevanje smatanja
proteina, ali i razvijanje metoda za liječenje neurodegenerativnih bolesti uzrokovanih
agregacijama proteina.

Abstract (english)

Chaperone Hsp90 is one of key regulators of proteostasis under both physiological and stress
conditions in eukaryotic cells. Members of Hsp90 protein family can be found in bacteria, cytosol,
endoplasmatic reticulum, mitochondria and chloroplast. All homologs exhibit similar structures
and functions because Hsp90 family is highly conserved. It forms complexes with its substrates
and enables their conformational rearrangements and gaining of an active protein structure. An
important role is played by co-chaperones that interact with the chaperone and regulate ATPase
activity, the conformational cycle of the Hsp90 dimer and interaction with other chaperones.
Hsp90 can also play the role of buffering and potentiating genetic variations and stimulating
novelty in evolution. Understanding the dynamics of Hsp90 and co-chaperones enables the
understanding of protein folding, but also the development of methods for the treatment of
neurodegenerative diseases caused by protein aggregation.

• Keywords: Hsp90; čaperon; kočaperon; evolucija
• Keywords (english): Hsp90; chaperone; co-chaperone; evolution
• Language: croatian
• URN:NBN: urn:nbn:hr:217:994660
• Study programme: Title: Molecular Biology; Study programme type: university; Study level: undergraduate; Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) molekularne biologije)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Open access
• Created on: 2022-10-13 11:45:27