Arrangement of the subunits in the ribosome of Escherichia coli: demonstration by immunoelectron microscopy.
AUTOR(ES)
Kastner, B
RESUMO
The three-dimensional locations of Escherichia coli ribosomal proteins S13, L1, and L7/L12 on the surface of ribosomal subunits and 70S monomeric ribosomes were determined by electron microscopy of antibody-labeled ribosomal particles. A new approach to orient the subunits within 70S ribosomes was developed that used 30S.70S.50S triples that were prepared by simultaneous combination with one antibody directed against a 30S protein and another directed against a 50S protein. Electron microscope studies of triples obtained with the antibody combinations anti-S13/anti-L1 and anti-S13/anti-L7/L12 showed that, in 70S monomeric ribosomes, the head of the 30S subunit is proximate to protein L1 and the peptidyl transferase center but far from the rod-like appendage containing proteins L7 and L12.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=349107Documentos Relacionados
- Membrane localization of the HflA regulatory protease of Escherichia coli by immunoelectron microscopy.
- Localization of yeast RNA polymerase I core subunits by immunoelectron microscopy.
- Architecture of the Escherichia coli ribosome as determined by immune electron microscopy.
- Capsule of Escherichia coli K29: ultrastructural preservation and immunoelectron microscopy.
- Comparison of Artemia salina and Escherichia coli ribosome structure by electron microscopy.
