Correction
for
Meriin et al., J. Cell Biol. 157 (6) 997-1004.
Published 5 August 2002. doi:10.1083/jcb.20020722157997
© The Rockefeller University Press,
0021-9525/2002/8/591 $5.00
The Journal of Cell Biology, Volume 158, Number 3, August 5, 2002 591-591
Meriin et al. Vol. 157, No. 6, June 10, 2002. Pages 997–1004.
The following paragraph contains a citation (Osherovich and Weissman, 2001) mistakenly omitted in the original publication of the article.
Our data that the polypeptide with expanded polyQ forms inclusions only in the presence of the [RNQ+] prion are consistent with the latest report showing that aggregation of the MJD protein with polyQ expansion is facilitated in so-called [PIN+] cells (Osherovich and Weissman, 2001). [PIN+] is a non-Mendelian genetic trait promoting emergence of [PSI+] (Derkatch et al., 1997; Osherovich and Weissman, 2001). It was shown that [PIN+] may be caused by a number of potential prion-forming proteins, for example, Rnq1 and New1 (Derkatch et al., 2001). Interestingly, deletion of the NEW1 gene did not significantly affect aggregation of 103Q polypeptide, suggesting the major role of [RNQ+] prion in this process. Whether aggregates of prion form of Rnq1, which has a QN-rich domain, could directly serve as a nucleation site for polyQ, or Rnq1 acts on the polyQ aggregation indirectly is yet to be established.
References
Osherovich, L.Z., and J.S. Weissman. 2001. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell. 106:183–194.[CrossRef][Medline]
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