Komparativna analiza fosfoproteoma sojeva bakterije S. rimosus koji proizvode oksitetraciklin

doctoral thesis

• Title (english): Comparative phosphoproteome analysis of Streptomyces rimosus oxytetracycline producers strains
• Author: Ela Šarić
• Mentor: Dušica Vujaklija (mentor)
• Committee member: Ksenija Zahradka (predsjednik povjerenstva)
• Committee member: Ivana Ivančić Baće (član povjerenstva)
• Committee member: Saša Kazazić (član povjerenstva)
• Granter: University of Zagreb; Faculty of Science; (Department of Biology); Zagreb
• Defense date and country: 2022-10-07, Croatia
• Scientific / art field, discipline and subdiscipline: NATURAL SCIENCES; Biology
• Universal decimal classification (UDC): 578/579 - Virology. Microbiology

Abstract

Streptomiceti su višestanične bakterije složenog životnog ciklusa. Najpoznatije su po
genetičkom potencijalu za sintezu antibiotika širokog spektra u koje spadaju i tetraciklini od
izuzetnog komercijalnog značaja. Već desetljećima se bakterija Streptomyces rimosus koristi
za proizvodnju oksitetraciklina (OTC) čija godišnja potrošnja prelazi 108
kg. Biosinteza
antibiotika je kontrolirana kompleksnim signalnim putevima koji uključuju i fosforilacije
proteina. Kako bi rasvijetlili regulatorne mehanizme uključene u procese odgovorne za rast i
sintezu OTC-a u ovoj doktorskoj radnji je primjenom spektrometrije masa po prvi put istražen
(fosfo)proteom bakterije S. rimosus G7 i visokog proizvođača OTC-a (soj 23383). Određena
je dinamika sinteze (fosfo)proteina tijekom rasta ovih bakterija, a ostvareni rezultati su
korelirani s procesima uključenim u biosintezu antibiotika i staničnu diferencijaciju.
Identificirano je 4053 proteina (~50% proteoma) te 433 fosfoproteina od kojih je 203
fosfoproteina pronađeno samo kod soja 23383. Funkcionalna karakterizacija i analiza dinamike
fosforilacije ovih proteina dali su posve novi uvid u fosfoproteom streptomiceta općenito.
Identificirana je do sada neopisana posttranslacijska modifikacija niza proteina koji su važni
za staničnu diobu i metabolizam te sintezu antibiotika i odgovor na stres.

Abstract (english)

Streptomycetes are multicellular bacteria with a complex life cycle. They are best known for
their great potential for the synthesis of broad-spectrum antibiotics, which include tetracyclines
of significant commercial importance. For decades, Streptomyces rimosus has been used to
produce oxytetracycline (OTC) whose annual consumption exceeds 108
kg. Antibiotic
biosynthesis is controlled by complex signaling pathways that include protein phosphorylation.
In order to elucidate the regulatory mechanisms involved in the processes responsible for
bacterial growth and OTC synthesis, the (phospho)proteome of S. rimosus G7 and a high OTC
producer (strain 23383) was investigated for the first time using mass spectrometry in this
doctoral dissertation. The dynamics of (phospho)proteomes during the growth of these bacteria
was determined and results were correlated with the processes involved in antibiotic
biosynthesis and cell differentiation. In total, 4053 proteins (~ 50% of proteomes) and 433
phosphoproteins were identified, of which 203 phosphoproteins were found only in strain
23383. Functional characterization and analysis of phosphorylation dynamics of these proteins
gave a completely new insight into streptomycete phosphoproteins in general. So far
undescribed posttranslational modification of a number of proteins important for cell division
and metabolism, as well as antibiotic synthesis and stress response, has been identified.

• Keywords: bakterija Streptomyces rimosus; proteom; fosfoproteom; oksitetraciklin
• Keywords (english): Streptomyces rimosus; proteome; phosphoproteome; oxytetracycline
• Language: croatian
• URN:NBN: urn:nbn:hr:217:263138
• Promotion: 2022
• Study programme: Title: Biology; Study programme type: university; Study level: postgraduate; Academic / professional title: doktor/doktorica znanosti, područje prirodnih znanosti, polje biologija (doktor/doktorica znanosti, područje prirodnih znanosti, polje biologija)
• Type of resource: Text
• File origin: Born digital
• Access conditions: Embargoed access; Embargo expiration date: 2024-10-07
• Created on: 2022-11-17 11:45:33