Naslov
Nucleoside-diphosphate kinase Nme6 in humans and sponges

Autori
Ćetković, Helena ; Radić, Martina ; Ačkar, Lucija ; Herak Bosnar, Maja

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

Izvornik
13th Multinational Congress on Microscopy : Book of Abstracts / Gajović, Andreja ; Weber, Igor ; Kovačević, Goran ; Čadež, Vida ; Šegota, Suzana ; Peharec Štefanić, Petra ; Vidoš, Ana - Zagreb : Institut Ruđer Bošković ; Hrvatsko mikroskopijsko društvo, 2017, 202-203

ISBN
978-953-7941-19-2

Skup
13th Multinational Congress on Microscopy

Mjesto i datum
Rovinj, Hrvatska, 24.09.2017. - 29.09.2017

Vrsta sudjelovanja
Poster

Vrsta recenzije
Podatak o recenziji nije dostupan

Ključne riječi
Nme6 ; Nm23-H6 ; NDPK

Sažetak
Nucleoside-diphosphate kinases (Nme/Nm23/NDPK) constitute a family of evolutionary conserved enzymes involved in many crucial biological processes. Despite of intensive studies in the last two decades, their biochemical functions have not yet been fully elucidated. The family consists of ten members divided in two groups. Group I, which encompasses Nme1- Nme4, has been extensively studied, especially Nme1 in the context of metastasis formation and Nme2 which appears to be involved in cardiac diseases. The Group I members in humans are generally highly homologous among themselves and in comparison to their orthologues in other Metazoans. They all possess the NDP kinase activity in their hexameric form. The Group II members display a lower level of mutual homology and apparently do not possess the NDP kinase activity. Their multimeric structure has not yet been revealed. The Group II members emerged very early in the evolutionary history, especially the Nme5, Nme6 and Nme7 and, therefore, considered to be involved in crucial biological processes. Building upon our previous work on the human and sponge Nme family proteins, the aim of this study is resolving the structure, as well as biochemical and biological functions of the human Nme6 and its changes during evolution. For this purpose we have been analyzing in parallel the human and the sponge nme6 homologs. Sponges are regarded to be living fossils, and it is widely accepted that their genome and proteome structure did not change much in the last 500 million years. Therefore, they have probably preserved the genome and proteome structure of the common ancestor of all Metazoans. Subcellular localization studies using confocal scanning microscopy reviled that the human Nme6 colocalizes mainly with mitochondria, while the sponge variant colocalizes with early, late and recycling endosomes of human tumor cells although it has a putative mitochondrial signaling sequence. The sponge Nme6 protein does not possess the NDPK activity. Bioinformatical analyses of the intron and promoter regions also reviled significant differences between the two nme6 homologs. Our results suggest that nme6 203 gene/protein changed significantly during evolution probably along with its biochemical and biological function. This, however, needs to be confirmed by future experiments.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA