Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism.
Ribosomes have a characteristic protuberance termed the stalk, which is indispensable for ribosomal function. The ribosomal stalk has long been believed to be a pentameric protein complex composed of two sets of protein dimers, L12-L12, bound to a single anchor protein, although ribosomes carrying t...
| Main Authors: | , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2007
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| _version_ | 1826283075970007040 |
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| author | Maki, Y Hashimoto, T Zhou, M Naganuma, T Ohta, J Nomura, T Robinson, C Uchiumi, T |
| author_facet | Maki, Y Hashimoto, T Zhou, M Naganuma, T Ohta, J Nomura, T Robinson, C Uchiumi, T |
| author_sort | Maki, Y |
| collection | OXFORD |
| description | Ribosomes have a characteristic protuberance termed the stalk, which is indispensable for ribosomal function. The ribosomal stalk has long been believed to be a pentameric protein complex composed of two sets of protein dimers, L12-L12, bound to a single anchor protein, although ribosomes carrying three L12 dimers were recently discovered in a few thermophilic bacteria. Here we have characterized the stalk complex from Pyrococcus horikoshii, a thermophilic species of Archaea. This complex is known to be composed of proteins homologous to eukaryotic counterparts rather than bacterial ones. In truncation experiments of the C-terminal regions of the anchor protein Ph-P0, we surprisingly observed three Ph-L12 dimers bound to the C-terminal half of Ph-P0, and the binding site for the third dimer was unique to the archaeal homologs. The stoichiometry of the heptameric complex Ph-P0(Ph-L12)(2)(Ph-L12)(2)(Ph-L12)(2) was confirmed by mass spectrometry of the intact complex. In functional tests, ribosomes carrying a single Ph-L12 dimer had significant activity, but the addition of the second and third dimers increased the activity. A bioinformatics analysis revealed the evidence that ribosomes from all archaeal and also from many bacterial organisms may contain a heptameric complex at the stalk, whereas eukaryotic ribosomes seem to contain exclusively a pentameric stalk complex, thus modifying our view of the stalk structure significantly. |
| first_indexed | 2024-03-07T00:53:28Z |
| format | Journal article |
| id | oxford-uuid:87327e7b-a3c7-45ee-9e9a-e6619acab9a5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:53:28Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:87327e7b-a3c7-45ee-9e9a-e6619acab9a52022-03-26T22:09:12ZThree binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:87327e7b-a3c7-45ee-9e9a-e6619acab9a5EnglishSymplectic Elements at Oxford2007Maki, YHashimoto, TZhou, MNaganuma, TOhta, JNomura, TRobinson, CUchiumi, TRibosomes have a characteristic protuberance termed the stalk, which is indispensable for ribosomal function. The ribosomal stalk has long been believed to be a pentameric protein complex composed of two sets of protein dimers, L12-L12, bound to a single anchor protein, although ribosomes carrying three L12 dimers were recently discovered in a few thermophilic bacteria. Here we have characterized the stalk complex from Pyrococcus horikoshii, a thermophilic species of Archaea. This complex is known to be composed of proteins homologous to eukaryotic counterparts rather than bacterial ones. In truncation experiments of the C-terminal regions of the anchor protein Ph-P0, we surprisingly observed three Ph-L12 dimers bound to the C-terminal half of Ph-P0, and the binding site for the third dimer was unique to the archaeal homologs. The stoichiometry of the heptameric complex Ph-P0(Ph-L12)(2)(Ph-L12)(2)(Ph-L12)(2) was confirmed by mass spectrometry of the intact complex. In functional tests, ribosomes carrying a single Ph-L12 dimer had significant activity, but the addition of the second and third dimers increased the activity. A bioinformatics analysis revealed the evidence that ribosomes from all archaeal and also from many bacterial organisms may contain a heptameric complex at the stalk, whereas eukaryotic ribosomes seem to contain exclusively a pentameric stalk complex, thus modifying our view of the stalk structure significantly. |
| spellingShingle | Maki, Y Hashimoto, T Zhou, M Naganuma, T Ohta, J Nomura, T Robinson, C Uchiumi, T Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title | Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title_full | Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title_fullStr | Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title_full_unstemmed | Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title_short | Three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism. |
| title_sort | three binding sites for stalk protein dimers are generally present in ribosomes from archaeal organism |
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