Duplikacije gena za aminoacil-tRNA-sintetaze i njihove raznolike uloge u bakterijama

undergraduate thesis

• Title (english): Aminoacyl-tRNA-sythetase gene duplications and their diverse roles in bacteria
• Author: Kian Bigović Villi
• Mentor: Ita Gruić-Sovulj (mentor)
• Granter: University of Zagreb; Faculty of Science; (Department of Biology); Zagreb
• Defense date and country: 2022-08-29, Croatia
• Scientific / art field, discipline and subdiscipline: NATURAL SCIENCES; Biology

Abstract

Aminoacil-tRNA-sintetaze (aaRS) su skupina enzima koja služi u prevođenju informacije zapisane u
nukleinskim kiselinama u informaciju zapisanu u polipeptidnim lancima. Njihova kanonska uloga u
bakterijskoj stanici obuhvaća stvaranje aminoacil-tRNA, sparivanjem aminokiseline i pripadne molekule
tRNA s visokim stupnjem točnosti. Tako nastala aminoacil-tRNA ribosomima služi kao supstrat za sintezu
proteina u procesu translacije. Uslijed mnoštva genskih duplikacija i horizontalnih prijenosa gena, neke
bakterije stekle su do dva dodatna gena koja kodiraju određenu aaRS. Iako naizgled suvišne, dodatne aaRS
pokazale su mnoštvo različitih nekanonskih funkcija koje danim bakterijama donose kompetitivnu prednost.
Kako su aaRS zbog svoje esencijalne kanonske uloge često meta antibiotika, mnoge bakterije stekle su
dodatnu aaRS otpornu na djelovanje danih antibiotika, induciranu njihovom prisutnošću. Takve aaRS
nerijetko se nalaze u okviru genskih klastera za biosintezu pripadnih antibiotika, te bakteriju štite
proizvedenog antibiotika, a nerijetko imaju ulogu i u samom biosintetskom procesu. Neke dodatne aaRS su
pak postale dio regulatornih sustava procesa sporulacije, dok su druge postale dio bakterijskih odgovora na
povišenu temperaturu, niski pH i prisustvo D-aminokiselina. Daljnje proučavanje duplikacija gena za aaRS
je od izrazite važnosti jer nosi potencijal za otkriće novih antibiotika i mehanizama otpornosti na njih, ali i
saznanja o temeljnim bakterijskim procesima.

Abstract (english)

Aminoacyl-tRNA-synthetases (aaRS) are enzymes that translate the information written in nucleic acids to
the information contained in polypeptide chains. Canonically, they catalyse the synthesis of
aminoacyl-tRNA, accurately pairing amino acids with the corresponding tRNA molecules. Obtained
aminoacyl-tRNAs are central to the process of translation as substrates in the ribosome-mediated protein
synthesis. Resulting from numerous gene duplications and horizontal transfers, some bacteria have acquired
up to 2 additional genes coding for a particular aaRS. Although seemingly redundant, these additional aaRSs
have shown a multitude of different non-canonical functions that confer various competitive advantages. As
aaRS are often targets of antibiotic activity, many bacteria have acquired additional, antibiotic-resistant
aaRSs induced in their presence. Such aaRSs are usually found within biosynthetic gene clusters for the
corresponding antibiotics where they serve to protect the bacteria from the produced antibiotic, while few
even have a role in the biosynthetic proces. Some additional aaRSs have become parts of a regulatory
network governing bacterial sporulation, while others integrated in bacterial responses to elevated
temperature, low pH and D-amino acids. Further studies of additional aaRSs are of particular importance,
as they may lead to the discovery of new antibiotics and antibiotic resistance mechanisms and elucidate
fundamental bacterial processes.

• Keywords: antibiotska rezistencija; odgovor na stres; sekundarni metaboliti; biosintetski klasteri; Strepromyces
• Keywords (english): antibiotic resistance; stress response; secondary metabolite; biosynthetic cluster; Strepromyces
• Language: croatian
• URN:NBN: urn:nbn:hr:217:785279
• 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: 2022-09-26 14:44:07