Ribosomal protein S1 in archaea.
Cell extracts and ribosomes of thermoacidophilic and halophilic archaebacteria were analysed by immunoblotting to detect ribosomal protein S1 homologues. Antisera to E. coli S1, the N-terminal ribosome binding domain (F2a) and the central and COOH-terminal nucleic acid binding domain (S1F1) of the protein were used. The results show that the thermoacidophilic archaebacterium sulfolobus acidocaldarius contains a protein with molecular weight of 66,000 that cross-reacts with anti-S1F1. However, the halophilic archaebacteria Halobacterium halobium, H. cutirubrum and H. salinarum contain a protein of molecular weight of about 100,000 that cross-reacts only with anti-F2a. The results indicate a differential conservation of the structural and functional domains of protein S1 in archaebacteria.
Department of Biochemistry, School of Life Sciences, University Hyderabad, India.
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Ravi
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Suryanarayana
D001105:Archaea / Q000737:chemistry*; D003429:Cross Reactions; D019617:Halobacterium salinarum / Q000737:chemistry; D015151:Immunoblotting; D008970:Molecular Weight; D012269:Ribosomal Proteins / Q000032:analysis* / Q000235:genetics / Q000276:immunology
D012269:Ribosomal Proteins; C015494:ribosomal protein S1