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http://purl.uniprot.org/citations/1541288http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1541288http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1541288http://www.w3.org/2000/01/rdf-schema#comment"The amino acid hypusine is formed by post-translational modification of a lysine residue in eukaryotes and archaebacteria but up to now only the eukaryotic translation initiation factor eIF-5A has been known to contain this unique component. We isolated and purified a hypusine-containing protein from the thermophilic archaebacterium Sulfolobus acidocaldarius. The mainly cytosolic protein comprised about 0.03% of the post-ribosomal supernatant protein. No other hypusine-containing protein could be detected in S. acidocaldarius. The molar ratio of hypusine/hypusine-containing protein was 1:1. SDS/PAGE showed a molecular mass of 16.8 kDa; a pI of 7.8 for the native protein resulted from IEF. The N-terminus was blocked. Four cyanogen bromide fragments were partially sequenced and used to derive two 17-base oligonucleotide probes. A 3-kb HindIII fragment of genomic DNA hybridizing with both probes was cloned. By sequencing of exonuclease III deletion clones an open reading frame of 405 nucleotides was found coding for a protein of 135 amino acids with a molecular mass of 15 kDa. It contained all cyanogen bromide sequences analysed. Sequence alignment revealed that seven of eight residues around Lys40 in the Sulfolobus hypusine-containing protein were identical to the nonapeptides centered by hypusine in the three eIF-5A proteins sequenced so far. The Edman procedure gave no phenylthiohydantoin derivative for this position. For a central region of 44 residues a sequence similarity of 54% between the archaebacterial and eukaryotic proteins was calculated; for the total sequence about 33% similarity resulted. In addition, there were a number of conservative changes. The unique lysine modification surrounded by a conserved sequence strongly suggests a common ancestry of archaebacterial hypusine-containing protein and eIF-5A. Together with similarities in molecular mass and intracellular localization, it may point to an analogous biochemical function."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb16690.x"xsd:string
http://purl.uniprot.org/citations/1541288http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1992.tb16690.x"xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Frank J."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Frank J."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Klink F."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Klink F."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Bartig D."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Bartig D."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Lemkemeier K."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/author"Lemkemeier K."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/pages"751-758"xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/pages"751-758"xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/title"The archaebacterial hypusine-containing protein. Structural features suggest common ancestry with eukaryotic translation initiation factor 5A."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/title"The archaebacterial hypusine-containing protein. Structural features suggest common ancestry with eukaryotic translation initiation factor 5A."xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/volume"204"xsd:string
http://purl.uniprot.org/citations/1541288http://purl.uniprot.org/core/volume"204"xsd:string
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