Pregled bibliografske jedinice broj: 1219541
PROTEOLYTIC PROCESSING AND COVALENT BINDING OF YEAST CELL WALL PROTEIN Scw10
PROTEOLYTIC PROCESSING AND COVALENT BINDING OF YEAST CELL WALL PROTEIN Scw10 // HDBMB22 From Science to Knowledge / Dulić, Morana ; Sinčić, Nino ; Vrhovac Madunić, Ivana (ur.).
Zagreb: Hrvatsko Društvo za Biotehnologiju, 2022. str. 101-101 (poster, nije recenziran, sažetak, znanstveni)
CROSBI ID: 1219541 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
PROTEOLYTIC PROCESSING AND COVALENT BINDING OF YEAST
CELL WALL PROTEIN Scw10
Autori
Lozančić, Mateja ; Grbavac, Antonija ; Matičević, Ana ; Hrestak, Dora ; Teparić, Renata ; Mrša, Vladimir
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
HDBMB22 From Science to Knowledge
/ Dulić, Morana ; Sinčić, Nino ; Vrhovac Madunić, Ivana - Zagreb : Hrvatsko Društvo za Biotehnologiju, 2022, 101-101
Skup
Congress of the Croatian Society of Biochemistry and Molecular Biology: From Science to Knowledge (HDBMB22)
Mjesto i datum
Brela, Hrvatska, 28.09.2022. - 01.10.2022
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
Kex2, yapsins, Scw4, Scw10, cell wall
Sažetak
The proteins Scw4, Scw10, and Scw11 form a group of putative glucanases found in the yeast cell wall. SCW4 and SCW10 are paralogous genes with very high sequence identity. It has been previously shown that Scw4 undergoes complex proteolytic processing that affects its biological function. Scw4 is first processed by the Kex2 protease in the Golgi and then by yapsin proteases located in the cell membrane and/or cell wall. This two-step processing has been reported to affect its activity and cell wall binding. Scw10 is known to have a Kex2 recognition site, but its proteolytic processing has not been thoroughly investigated. It has also been shown that both Scw4 and Scw10 can form non-covalent and covalent bonds with the wall. The covalent bond is of particular interest because it differs from other previously known bonds in the cell wall. Although it has similar properties to the bonds formed by Pir family proteins, both Scw4 and Scw10 lack the typical Pir binding sequence. Therefore, the binding sequence and mechanism of Scw4 and Scw10 remain unknown. Here we present results obtained by studying the processing of Scw10. They show that the processing is similar in complexity to that of Scw4 but differs in terms of processing sites. The role of several putative Scw4/Scw10 binding sequences in forming a covalent bond to cell wall structures has been discussed.
Izvorni jezik
Engleski
Znanstvena područja
Biotehnologija
POVEZANOST RADA
Projekti:
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)
IP-2019-04-2891 - Biotehnološka primjena ugradnje heterolognih proteina u stanične stijenke kvasaca (PRODIS) (Mrša, Vladimir, HRZZ - 2019-04) ( CroRIS)
Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb
Profili:
Dora Hrestak
(autor)
Vladimir Mrša
(autor)
Renata Teparić
(autor)
Mateja Lozančić
(autor)
Antonija Grbavac
(autor)