HMGB2 Protein from the Marine Sponge Suberites domuncula
Investigation of the phylogenetically conserved genes/proteins from marine sponges (Porifera), the most primitive metazoan phylum, can be applied for the reconstruction of ancient structures of genome/proteom complexity in the ancestral organism common to all multicellular animals. The complete nucl...
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doaj-81d7f8b9271f402ba8ffa3d907a574ba2020-11-25T02:52:10ZengUniversity of ZagrebFood Technology and Biotechnology1330-98621334-26062003-01-01414361365HMGB2 Protein from the Marine Sponge Suberites domunculaLada Lukić-Bilela0Helena Ćetković1Department of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, HR-10000 Zagreb, CroatiaDepartment of Molecular Biology, Ruđer Bošković Institute, Bijenička 54, HR-10000 Zagreb, CroatiaInvestigation of the phylogenetically conserved genes/proteins from marine sponges (Porifera), the most primitive metazoan phylum, can be applied for the reconstruction of ancient structures of genome/proteom complexity in the ancestral organism common to all multicellular animals. The complete nucleotide sequence of Suberites domuncula (Demospongiae) cDNA coding for 183-amino-acid protein (21.3 kDa), which displays high overall similarity in primary structure and organization of domains with HMGB canonical proteins, belonging to High Mobility Group (HMG) family of nuclear proteins, is reported here. The major role of these non-specific DNA binding proteins is to facilitate the formation of complex nucleoprotein assemblies and nucleosome remodelling. The encoded protein, named HMGB2SD, contains two typical, highly conserved DNA-binding domains: box A (69 aa) and box B (71 aa). Short C-terminal »tail« is only 13 aa long. HMG2SD displays the highest overall similarity (58 %) with HMGB2 proteins from mammals (pig, human, rat, mouse), higher than with Drosophila melanogaster (53 %) or Caenorhabditis elegans (31 %) homologues. This is in accordance with previous results, which showed the best homology between sponge and mammalian homologues/ortologues. Our results further confirm that sponges are an excellent model for molecular evolutionary studies.http://hrcak.srce.hr/file/185089PoriferaSuberites domunculaHigh Mobility Group proteinsHMGB2molecular evolution |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lada Lukić-Bilela Helena Ćetković |
spellingShingle |
Lada Lukić-Bilela Helena Ćetković HMGB2 Protein from the Marine Sponge Suberites domuncula Food Technology and Biotechnology Porifera Suberites domuncula High Mobility Group proteins HMGB2 molecular evolution |
author_facet |
Lada Lukić-Bilela Helena Ćetković |
author_sort |
Lada Lukić-Bilela |
title |
HMGB2 Protein from the Marine Sponge Suberites domuncula |
title_short |
HMGB2 Protein from the Marine Sponge Suberites domuncula |
title_full |
HMGB2 Protein from the Marine Sponge Suberites domuncula |
title_fullStr |
HMGB2 Protein from the Marine Sponge Suberites domuncula |
title_full_unstemmed |
HMGB2 Protein from the Marine Sponge Suberites domuncula |
title_sort |
hmgb2 protein from the marine sponge suberites domuncula |
publisher |
University of Zagreb |
series |
Food Technology and Biotechnology |
issn |
1330-9862 1334-2606 |
publishDate |
2003-01-01 |
description |
Investigation of the phylogenetically conserved genes/proteins from marine sponges (Porifera), the most primitive metazoan phylum, can be applied for the reconstruction of ancient structures of genome/proteom complexity in the ancestral organism common to all multicellular animals. The complete nucleotide sequence of Suberites domuncula (Demospongiae) cDNA coding for 183-amino-acid protein (21.3 kDa), which displays high overall similarity in primary structure and organization of domains with HMGB canonical proteins, belonging to High Mobility Group (HMG) family of nuclear proteins, is reported here. The major role of these non-specific DNA binding proteins is to facilitate the formation of complex nucleoprotein assemblies and nucleosome remodelling. The encoded protein, named HMGB2SD, contains two typical, highly conserved DNA-binding domains: box A (69 aa) and box B (71 aa). Short C-terminal »tail« is only 13 aa long. HMG2SD displays the highest overall similarity (58 %) with HMGB2 proteins from mammals (pig, human, rat, mouse), higher than with Drosophila melanogaster (53 %) or Caenorhabditis elegans (31 %) homologues. This is in accordance with previous results, which showed the best homology between sponge and mammalian homologues/ortologues. Our results further confirm that sponges are an excellent model for molecular evolutionary studies. |
topic |
Porifera Suberites domuncula High Mobility Group proteins HMGB2 molecular evolution |
url |
http://hrcak.srce.hr/file/185089 |
work_keys_str_mv |
AT ladalukicbilela hmgb2proteinfromthemarinespongesuberitesdomuncula AT helenacetkovic hmgb2proteinfromthemarinespongesuberitesdomuncula |
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1724730842313392128 |