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- W2398564868 abstract "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." @default.
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- W2398564868 date "1994-10-01" @default.
- W2398564868 modified "2023-09-27" @default.
- W2398564868 title "Ribosomal protein S1 in archaea." @default.
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