Reference - PMID:15802566 - Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.
Reference summary
- PubMed ID
- PMID:15802566
- Title
- Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous.
- Authors
- Hundley HA, Walter W, Bairstow S, Craig EA
- Citation
- Science 2005 May 13;308(5724):1032-4
- Publication year
- 2005
- Abstract
- The existence of specialized molecular chaperones that interact directly with ribosomes is well established in microorganisms. Such proteins bind polypeptides exiting the ribosomal tunnel and provide a physical link between translation and protein folding. We report that ribosome-associated molecular chaperones have been maintained throughout eukaryotic evolution, as illustrated by Mpp11, the human ortholog of the yeast ribosome-associated J protein Zuo. When expressed in yeast, Mpp11 partially substituted for Zuo by partnering with the multipurpose Hsp70 Ssa, the homolog of mammalian Hsc70. We propose that in metazoans, ribosome-associated Mpp11 recruits the multifunctional soluble Hsc70 to nascent polypeptide chains as they exit the ribosome.
