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

Hendrik Otta, Charlotte Conz, Philipp Maier, Tina Wölfle, Carolyn K. Suzuki, Paul Jenö, Peter Rücknagel, Joachim Stahl, Sabine Rospert

Research output: Contribution to journalArticlepeer-review

99 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)10064-10069
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume102
Issue number29
DOIs
StatePublished - Jul 19 2005

All Science Journal Classification (ASJC) codes

  • General

Keywords

  • Myb domain
  • NatA
  • Protein folding
  • Translation

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