Nalazite se na CroRIS probnoj okolini. Ovdje evidentirani podaci neće biti pohranjeni u Informacijskom sustavu znanosti RH. Ako je ovo greška, CroRIS produkcijskoj okolini moguće je pristupi putem poveznice www.croris.hr
izvor podataka: crosbi !

Identification of novel interacting partners: what can we learn from native protein complexes? (CROSBI ID 566030)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija

Jurić, Snježana ; Horvat, Lucija ; Tomašić, Ana ; Fulgosi, Hrvoje Identification of novel interacting partners: what can we learn from native protein complexes? // The secret life of biomolecules / Kovarnik, Zrinka ; Varljen, Jadranka (ur.). Rijeka: Hrvatsko Društvo za Biotehnologiju, 2010. str. 81-81

Podaci o odgovornosti

Jurić, Snježana ; Horvat, Lucija ; Tomašić, Ana ; Fulgosi, Hrvoje

engleski

Identification of novel interacting partners: what can we learn from native protein complexes?

Photosynthesis is a highly complex and versatile network of processes performed by multiprotein complexes associated with pigment molecules. Although the structure and role of nearly all subunits of the major thylakoid complexes are discovered, the large-scale proteomic approaches identified a great number of so-called auxiliary proteins with completely uninvestigated roles in photosynthesis. In our previous research we demonstrated that the novel thylakoid protein designated TROL (the Thylakoid Rhodanese-Like protein), is located almost exclusively in the non-appressed thylakoids, predicting to face the stroma with its C-terminus, encompassing the ITEP domain, and to expose the central part to the lumen, encompassing the RHO domain. The yeast two-hybrid and coimmunoprecipitation experiments univocally showed that ITEP interacts with the FNR protein, known to be involved in final transfer of electrons from ferredoxin to NADP+ molecule. The RHO domain shares the rhodanese-like three-dimensional fold with the regulatory domains from the Cdc25 phosphatases. Functional rhodanese domains have a cysteine residue in the active-site, which enables them to participate in sulphur metabolism, while the RHO domain contains an aspartic acid residue instead of the cysteine. To question the possible role of RHO in the signalling across the chloroplast and towards the nucleus (the retrograde signalling), the trol plants were complemented with the modified versions of the TROL protein. Isolation of the thylakoid multiprotein complexes in their native state revealed that TROL is assembled in four complexes, at 420 kDa, 190 kDa, 120 and 110 kDa, respectively. The mass spectrometry analysis of the TROL-containing complexes identified a few possible interacting candidates which will be thoroughly investigated.

FNR; Plant; Rhodanese

Predavanje u sklopu dodjele nagrade HDBMB-a mladim znanstvenicima za najbolji rad u 2009. godini.

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

Podaci o prilogu

81-81.

2010.

objavljeno

Podaci o matičnoj publikaciji

The secret life of biomolecules

Kovarnik, Zrinka ; Varljen, Jadranka

Rijeka: Hrvatsko Društvo za Biotehnologiju

Podaci o skupu

10th congress of the Croatian society of biochemistry and molecular biology

predavanje

15.09.2010-18.09.2010

Opatija, Hrvatska

Povezanost rada

Biologija