DOI: 10.1073/pnas.0504400102. The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex

The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex

10.1073/pnas.0504400102

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Soluble Hsp70 homologs cotranslationally interact with nascent polypeptides in all kingdoms of life. In addition, fungi possess a specialized Hsp70 system attached to ribosomes, which in Saccharomyces cerevisiae consists of the Hsp70 homologs Ssb1/2p, Ssz1p, and the Hsp40 homolog zuotin. Ssz1p and zuotin are assembled into a unique heterodimeric complex termed ribosome-associated complex. So far, no such specialized chaperones have been identified on ribosomes of higher eukaryotes. However, a family of proteins characterized by an N-terminal zuotin-homology domain fused to a C-terminal two-repeat Myb domain is present in animals and plants. Members of this family, like human MPP11 and mouse MIDA1, have been implicated in the regulation of cell growth. Specific targets of MPP11/MIDA1, however, have remained elusive. Here, we report that MPP11 is localized to the cytosol and associates with ribosomes. Purification of MPP11 revealed that it forms a stable complex with Hsp70L1, a distantly related homolog of Ssz1p. Complementation experiments indicate that mammalian ribosome-associated complex is functional in yeast. We conclude that despite a low degree of homology on the amino acid level cooperation of ribosome-associated chaperones with the translational apparatus is well conserved in eukaryotic cells.

Bibliography

Otto, H., Conz, C., Maier, P., WÃ¶lfle, T., Suzuki, C. K., JenÃ¶, P., RÃ¼cknagel, P., Stahl, J., & Rospert, S. (2005). The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proceedings of the National Academy of Sciences, 102(29), 10064â10069.

Authors 9

Hendrik Otto (first)
Charlotte Conz (additional)
Philipp Maier (additional)
Tina Wölfle (additional)
Carolyn K. Suzuki (additional)
Paul Jenö (additional)
Peter Rücknagel (additional)
Joachim Stahl (additional)
Sabine Rospert (additional)

References 46 Referenced 117

Rospert, S., Gautschi, M., Rakwalska, M. & Raue, U. (2005) in Protein Folding Handbook, eds. Buchner, J. & Kiefhaber, T. (Wiley, Weinheim, Germany), Vol. II, pp. 429-458. / Protein Folding Handbook (2005)
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Dates

Type	When
Created	20 years, 1 month ago (July 7, 2005, 8:34 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 1:33 p.m.)
Indexed	1 month, 2 weeks ago (July 12, 2025, 6:48 p.m.)
Issued	20 years, 1 month ago (July 7, 2005)
Published	20 years, 1 month ago (July 7, 2005)
Published Online	20 years, 1 month ago (July 7, 2005)
Published Print	20 years, 1 month ago (July 19, 2005)

Funders 0

None

BibTeX

@article{Otto_2005, title={The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex}, volume={102}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0504400102}, DOI={10.1073/pnas.0504400102}, number={29}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Otto, Hendrik and Conz, Charlotte and Maier, Philipp and Wölfle, Tina and Suzuki, Carolyn K. and Jenö, Paul and Rücknagel, Peter and Stahl, Joachim and Rospert, Sabine}, year={2005}, month=jul, pages={10064–10069} }

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