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 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

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 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

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 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

A young researcher’s guide to NME/Nm23/NDP Kinase

Nucleoside diphosphate kinases (NDPKs) catalyze the exchange of the terminal phosphate from trinucleotides to dinucleotides through a high-energy phosphohistidine intermedier. They are encoded by NME genes and have been found, with a few exceptions, in all living beings. Besides their well-known function as key regulators of the cellular nucleotide homeostasis, they have been appointed numerous additional biochemical and biological functions. The discovery of NME1/NDPK A as the first metastasis suppressor opened new avenues in cancer research. Although the precise role of NME genes/proteins in cancer dissemination is not yet revealed, it seems that further intensive research in this field may lead to new advances in cancer diagnosis and prognosis, as well as encourage new therapeutic strategies.</p

Sponges: A Reservoir of Genes Implicated in Human Cancer

Recently, it was shown that the majority of genes linked to human diseases, such as cancer genes, evolved in two major evolutionary transitions—the emergence of unicellular organisms and the transition to multicellularity. Therefore, it has been widely accepted that the majority of disease-related genes has already been present in species distantly related to humans. An original way of studying human diseases relies on analyzing genes and proteins that cause a certain disease using model organisms that belong to the evolutionary level at which these genes have emerged. This kind of approach is supported by the simplicity of the genome/proteome, body plan, and physiology of such model organisms. It has been established for quite some time that sponges are an ideal model system for such studies, having a vast variety of genes known to be engaged in sophisticated processes and signalling pathways associated with higher animals. Sponges are considered to be the simplest multicellular animals and have changed little during evolution. Therefore, they provide an insight into the metazoan ancestor genome/proteome features. This review compiles current knowledge of cancer-related genes/proteins in marine sponges

Rho Family of Ras-Like GTPases in Early-Branching Animals

Non-bilaterian animals consist of four phyla ; Porifera, Cnidaria, Ctenophora, and Placozoa. These early-diverging animals are crucial for understanding the evolution of the entire animal lineage. The Rho family of proteins make up a major branch of the Ras superfamily of small GTPases, which function as key molecular switches that play important roles in converting and amplifying external signals into cellular responses. This review represents a compilation of the current knowledge on Rho-family GTPases in non-bilaterian animals, the available experimental data about their biochemical characteristics and functions, as well as original bioinformatics analysis, in order to gain a general insight into the evolutionary history of Rho-family GTPases in simple animals

Genetics of Marine Organisms Associated with Human Health

Marine habitats harbour a large variety of organisms that belong to diverse taxa ; from bacteria and unicellular eukaryotes to fungi, animals, and plants. Although we have only started to understand the diversity and structure of marine communities, it is clear that numerous marine species have or might have an impact on human health. Some are a source of natural products with potential or actual medical applications, others are toxic and harmful to humans, and some are used in biomedical research to help understand the molecular basis of human diseases. New molecular genetics and genomic methods provide powerful and ever more indispensable tools for studying marine organisms and all aspects of their influence on human health. Herein, we present work using the latest research, which mostly uses genomics, to tackle the questions related with the topic of the issue

Dvije nukleozid-difosfat kinaze (NDPK/Nm23) iz morske spužve Suberites domuncula

Suberites domuncula is a member of the most ancient and simplest extant phylum of multicellular animals – sponges (Porifera). A database of S. domuncula expressed sequence tags (ESTs) was recently constructed by random cDNA sequencing. Two NDPK/Nm23 proteins from the sponge Suberites domuncula are reported here. Sponge proteins were named Nm23-SD1 and Nm23-SD6, because they display the highest sequence similarity with human Nm23-H1 and -H6 proteins. Overall sequence conservation of Nm23-SD1 with human Nm23-H1 is very high – 79 % (71 % identical amino acids). Nm23-SD6 possesses an insertion at the C-terminus and displays 55 % overall homology (40 % identical amino acids) with human Nm23 H6. Secondary structure predictions for both sponge and human Nm23 protein pairs are almost identical. S. domuncula Nm23 proteins display high similarity to homologues from mammals/humans, higher than to e.g. NDPK/Nm23 proteins from Drosophila or other invertebrates. Sponge Nm23 proteins are more similar to mammalian/human Nm23 proteins than most known Nm23 proteins of invertebrates.Suberites domuncula je pripadnik najstarije i najjednostavnije postojeće skupine (koljena) višestaničnih životinja – spužvi (Porifera). Nasumičnim sekvenciranjem cDNA S. domuncula nedavno je konstruirana baza EST-ova (expressed sequence tags). U ovom radu opisana su dva NDPK/Nm23 proteina iz spužve Suberites domuncula. Spužvini proteini nazvani su Nm23-SD1 i Nm23-SD6 jer su po aminokiselinskim sljedovima najslič niji ljudskim Nm23-H1 i -H6 proteinima. Ukupna sačuvanost sekvence izme|u Nm23-SD1 i Nm23-H1 vrlo je visoka i iznosi 79 % (71 % je identična). Nm23-SD6 ima inserciju na C-kraju i pokazuje ukupnu homologiju od 55 % (40 % identičnosti) s ljudskim Nm23-H6. Predikcija sekundarne strukture pokazuje da su oba proteinska para gotovo jednaka. Nm23 proteini iz spužve S. domuncula pokazuju visoku sličnost s homolozima iz sisavaca/čovjeka, višu nego s npr. NDPK/Nm23 proteinima iz vinske mušice ili drugih beskralješnjaka. Osim toga, sličniji su proteinima iz sisavaca/čovjeka od većine poznatih Nm23 proteina iz beskralješnjak