Open AccessUbiquitins (polyubiquitin and ubiquitin extension protein) in marine sponges: cDNA sequence and phylogenetic analysis
Author(s) -
WIENS MATTHIAS,
LUKIC LADA,
MÜLLER WERNER E.G.,
GAMULIN VERA
Publication year - 1999
Publication title -
biological journal of the linnean society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.906
H-Index - 112
eISSN - 1095-8312
pISSN - 0024-4066
DOI - 10.1111/j.1095-8312.1999.tb01928.x
Subject(s) - biology , complementary dna , translational frameshift , gene , ubiquitin , ribosomal protein , ubiquitins , genetics , phylogenetic tree , nucleic acid sequence , peptide sequence , biochemistry , microbiology and biotechnology , ubiquitin ligase , ribosome , open reading frame , rna
The complete nucleotide sequences of two Suberites domuncula cDNAs and one Sycon raphanus cDNA, all encoding ubiquitin, have been determined. One cDNA from S. domuncula codes for polyubiquitin with four tandemly repeated monomeric units and the second cDNA encodes ubiquitin fused to a ribosomal protein of 78 amino acids (aa). S. domuncula possesses at least one additional polyubiquitin gene, from which the last two monomers were also sequenced. All analysed genes from S. domuncula encode identical ubiquitin proteins, with only one aa difference (Ala 19) to the human/higher animals ubiquitin (Pro 19). Ubiquitin in S. domuncula is identical with the ubiquitin found in another Demospongia, Geodia cydonium. The cDNA from S. raphanus encodes polyubiquitin with seven tandemly repeated units. All these gene monomers code for the same ubiquitin, which differs from the human/higher animals ubiquitin only at position 24 (Asp in Sycon , Glu in others). However, ubiquitin from S. raphanus (Calcarea) shows two aa differences (positions 19 and 24), when compared with the ubiquitin sequences from the two Demospongiae. In a phylogenetic tree constructed by multiple sequence alignment of all sponge ubiquitin gene monomers so far identified, all monomers from the same species cluster together, with the clear exception of the monomer from S. domuncula ribosomal protein fusion gene. This monomer branches off first from the tree and forms a separate line; this gives evidence for a very ancient split of ubiquitin‐ribosomal‐protein fusion genes from polyubiquitin encoding genes and their long separate coexistence in eukaryotes. The ubiquitin extension protein from S. domuncula is 78 aa long, displays all characteristics of 76–81 aa long ribosomal fusion proteins and shows 78% identity in the first 73 aa with the human S27a protein. However, its C‐terminal sequence: 69‐GLTYVYKKSD‐78 is more similar to the plant consensus (69‐GLTYVYQ/NK‐76), than to the higher animal consensus (69‐CLTYCFNK‐76). This protein isolated from a sponge, belonging to the phylogenetically oldest multicellular animals, the Porifera, branches off first from the phylogenetic tree of metazoan ubiquitin extension proteins of the small ribosomal subunits.