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Published March 30, 1989 | public
Journal Article

The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis


Three of the four yeast ubiquitin genes encode hybrid proteins which are cleaved to yield ubiquitin and previously unidentified ribosomal proteins. The transient association between ubiquitin and these proteins promotes their incorporation into nascent ribosomes and is required for efficient ribosome biogenesis. These results suggest a novel 'chaperone' function for ubiquitin, in which its covalent association with other proteins promotes the formation of specific cellular structures.

Additional Information

© 1989 Nature Publishing Group. Received 12 December 1988; accepted 9 February 1989. We thank Mary Jalenak for assistance in characterizing mutants, John McGrath for carrying out sequence searches, Joan Park and Andreas Bachmair for helpful discussions, Vincent Chau for the anti-ubiquitin antibody, Tauseef Butt and David Ecker for the plasmid YEp46. Sean Munro for advice on peptide tagging, Brian Seed for advice on RNA electrophoresis, members of this laboratory for comments on the manuscript, Daniel Weeks and Douglas Melton for permission to cite unpublished data, and Barbara Doran for secretarial assistance. This work was supported by grants to A.V. from the NIH. B.B. was supported by a predoctoral fellowship from the NSF.

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