Pregled bibliografske jedinice broj: 1006230
Scw4 and Scw10 as new potential platforms for yeast cell surface expression systems
Scw4 and Scw10 as new potential platforms for yeast cell surface expression systems // Power of Microbes in Industry and Environment 2019, Book of Abstracts / Slavica, Anita ; Teparić, Renata ; Leboš Pavunc, Andreja ; Kifer, Domagoj (ur.).
Sveti Martin na Muri, Hrvatska, 2019. str. 44-44 (predavanje, nije recenziran, sažetak, znanstveni)
CROSBI ID: 1006230 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Scw4 and Scw10 as new potential platforms for yeast cell surface expression systems
Autori
Lozančić, Mateja ; Grbavac, Antonija ; Teparić, Renata ; Mrša, Vladimir
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Power of Microbes in Industry and Environment 2019, Book of Abstracts
/ Slavica, Anita ; Teparić, Renata ; Leboš Pavunc, Andreja ; Kifer, Domagoj - , 2019, 44-44
ISBN
978-953-7778-17-0
Skup
Power of Microbes in Industry and Environment 2019
Mjesto i datum
Sveti Martin na Muri, Hrvatska, 15.05.2019. - 18.05.2019
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Nije recenziran
Ključne riječi
yeast ; Scw4 ; Scw10 ; cell wall ; surface display
Sažetak
Yeast cell wall proteins can be used for surface display of various proteins of industrial interest. Generally, yeast cell wall contains proteins that are non-covalently (Scw- proteins) or covalently (Ccw-proteins) bound to β-1, 3-glucan, the latter either through GPI- anchors and β-1, 6-glucan, or by alkali labile ester linkages between γ-carboxyl groups of glutamic acid and hydroxyl groups of glucoses (Pir-proteins). Covalently bound proteins are usually used for immobilization of different recombinant proteins. Here we explore possibility of using Scw4 and Scw10 as novel immobilization platforms. Previously it was shown that Scw4 protein can be covalently and non-covalently linked to the cell wall structures. It was also shown that proteolytic processing of Scw4 by yapsins strongly affects its covalent binding. As Scw10 shares high level of similarity with Scw4, it is interesting to investigate whether Scw10 can also form both covalent and non-covalent interactions with cell wall structures. Although protein Scw10 also contains sequence charasteristic for Kex2 processing, it is not yet clearly confirmed whether Scw10 is substrate for Kex2. Furthermore, both of these proteins have potential to be used for development of new homologous and heterologous cell surface expression system for wide range of yeast species given that genomes of some other yeast species contain SCW4/SCW10 orthologs, as it is noted before. In order to develop Scw4/Scw10 based expression systems, further characterization of this two proteins is necessary. One line of the research was focused on Scw10 proteolytic processing. Results show that Scw10 undergoes processing by Kex2 and possibly by yapsins at the same site. Results also show that this processing doesn’t affect significantly Scw10 covalent binding efficiency. Other line of the research examines the level of evolutionary preservation of these proteins among different ascomycetes yeast by analysing cell wall protein profiles. Obtained results were coupled with results of in-sillico analysis of proteomes of different yeast species and it was found that Scw4 and Scw10 show high level of evolutionary preservation, given that all of analysed ascomycetes yeast, except two Schizosaccharomyces species, contained at least one protein with high similarity to them. Further research will focus on development of Scw4/Scw10 based expression system models and usage of this models in different yeast species
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
POVEZANOST RADA
Projekti:
HRZZ-IP-2014-09-2837 - Molekularni mehanizmi ugradnje homolognih i heterolognih proteina u staničnoj stijenci kvasca i njhova primjena (CEWAPROT) (Mrša, Vladimir, HRZZ - 2014-09) ( CroRIS)
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb
Profili:
Vladimir Mrša
(autor)
Renata Teparić
(autor)
Mateja Lozančić
(autor)
Antonija Grbavac
(autor)