Ribosomal proteins S2, S6, S10, S14, S15 and S25 are localized on the surface of mammalian 40 S subunits and stabilize their conformation A study with immobilized trypsin

Trypsin immobilized on collagen membranes has been used to digest accessible ribosomal proteins of rat liver 40 S subunits. Six proteins (S2, S6, S10, S14, S15 and S25) have been found to be highly exposed on the surface of 40 S particles. They appear to be in close physical contact and localized in...

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Bibliographic Details
Published in:FEBS letters 1988-05, Vol.232 (2), p.281-285
Main Authors: Marion, Marie-Jeanne, Marion, Christian
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Birefringence
Cell structures and functions
Electric birefringence
Electrophoresis
Enzymes, Immobilized
Fundamental and applied biological sciences. Psychology
Immobilized enzyme
Liver - analysis
Molecular and cellular biology
Protein Conformation
Rat liver
Rats
Rats, Inbred Strains
Ribosomal 40 S subunit
Ribosomal protein
Ribosomal Protein S6
Ribosomal Proteins - analysis
Ribosomal Proteins - metabolism
Ribosome
Trypsin
Trypsin - metabolism
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Summary:Trypsin immobilized on collagen membranes has been used to digest accessible ribosomal proteins of rat liver 40 S subunits. Six proteins (S2, S6, S10, S14, S15 and S25) have been found to be highly exposed on the surface of 40 S particles. They appear to be in close physical contact and localized in the same region of the subunit, most likely protruding at its surface. Electric birefringence reveals that digestion of these proteins results in unfolding of subunits: the birefringence of 40 S particles becomes negative, like that of RNA, the relaxation time undergoes a 15-fold decrease and the mechanism of orientation is drastically modified.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)80753-1