Naslov
Identification of novel interacting partners: what can we learn from the native protein complexes?
(Identification of novel interacting partners: what can we learn from native protein complexes?)

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

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
The secret life of biomolecules / Kovarnik, Zrinka ; Varljen, Jadranka - Rijeka : Hrvatsko Društvo za Biotehnologiju, 2010, 81-81

Skup
10th Congress of the Croatian Society of Biochemistry and Molecular Biology

Mjesto i datum
Opatija, Hrvatska, 15.09.2010. - 18.09.2010

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Domaća recenzija

Ključne riječi
FNR; Plant; Rhodanese

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

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

POVEZANOST RADA