PMID:2664451: Difference between revisions

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<span style = 'font-size: large'> '''Lotti, M, Noah, M, Stöffler-Meilicke, M and Stöffler, G'''  (1989) Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy.''Mol. Gen. Genet.'' '''216''':245-53</span>
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!align=left  |Citation
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'''No author listed'''  (1989) Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy. ''Mol. Gen. Genet.'' '''216''':245-53
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!align=left  |Abstract
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Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2664451 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.
!align=left  |Keywords
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Bacterial Proteins; Escherichia coli/ultrastructure; Escherichia coli Proteins; Immunochemistry; Microscopy, Electron; Protein Conformation; Ribosomal Proteins/immunology; Ribosomal Proteins/ultrastructure; Ribosomes/ultrastructure
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2664451 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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Revision as of 19:19, 1 September 2013

Citation

No author listed (1989) Localization of proteins L4, L5, L20 and L25 on the ribosomal surface by immuno-electron microscopy. Mol. Gen. Genet. 216:245-53

Abstract

Ribosomal proteins L4, L5, L20 and L25 have been localized on the surface of the 50S ribosomal subunit of Escherichia coli by immuno-electron microscopy. The two 5S RNA binding proteins L5 and L25 were both located at the central protuberance extending towards its base, at the interface side of the 50S particle. L5 was localized on the side of the central protuberance that faces the L1 protuberance, whereas L25 was localized on the side that faces the L7/L12 stalk. Proteins L4 and L20 were both located at the back of the 50S subunit; L4 was located in the vicinity of proteins L23 and L29, and protein L20 was localized between proteins L17 and L10 and is thus located below the origin of the L7/L12 stalk.

Links

PubMed

Keywords

Bacterial Proteins; Escherichia coli/ultrastructure; Escherichia coli Proteins; Immunochemistry; Microscopy, Electron; Protein Conformation; Ribosomal Proteins/immunology; Ribosomal Proteins/ultrastructure; Ribosomes/ultrastructure

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