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A more recent version of this article appeared on November 1, 2003
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Submitted on February 11, 2003
Revised on June 5, 2003
Accepted on June 26, 2003
1 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229 USA; Current address: Howard Hughes Medical Institute, Vollum Institute, Oregon Health & Science University, Portland, Oregon 97239, USA.
2 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229 USA
* Corresponding author. E-mail address: gsprague{at}molbio.uoregon.edu.
Ubiquitin is a small modifier protein which is conjugated to
substrates to target them for degradation. Recently a surprising number
of ubiquitin-like proteins have been identified that also can be
attached to proteins. Here we identify two molecular functions for the
posttranslational protein modifier from S. cerevisiae,
Urm1p. Simultaneous loss of Urm1p and Cla4p, a PAK kinase that
functions in budding, is lethal. This result suggests a role for the
urmylation pathway in budding. Furthermore, loss of the urmylation
pathway has defects in invasive growth and confers sensitivity to
rapamycin. Our results indicate that the sensitivity to rapamycin is
due to a genetic interaction with the TOR pathway, which is important
for regulation of cell growth in response to nutrients. We have found
that Urm1p can be attached to a number of proteins. Loss of five genes
that are also essential in a cla4
strain,
NCS2, NCS6, ELP2, ELP6 and URE2, affect the
level of at least one Urm1p conjugate. Moreover, these five genes have
a role in invasive growth and display genetic interactions with the TOR
pathway. In summary, our results suggest the urmylation pathway is
involved in nutrient sensing and budding.
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