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J. Biol. Chem., Vol. 275, Issue 32, 24921-24927, August 11, 2000
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From the Institute for Biochemistry, University of Munich
(LMU), Feodor-Lynen-Str. 25, D-81377 Munich, Germany,
§ Département de Microbiologie et Infectiologie,
Faculté de Médecine, Université de Sherbrooke,
Sherbrooke, Quebec J1H 5N4, Canada, and The Yku heterodimer from Saccharomyces
cerevisiae, comprising Yku70p and Yku80p, is involved in the
maintenance of a normal telomeric DNA end structure and is an essential
component of nonhomologous end joining (NHEJ). To investigate the role
of the Yku70p subunit in these two different pathways, we generated
C-terminal deletions of the Yku70 protein and examined their ability to
complement the phenotypes of a yku70
A Short C-terminal Domain of Yku70p Is Essential for Telomere
Maintenance*
,
, GSF-National
Research Center for Environment and Health, Institute of Molecular
Immunology, Marchioninistr. 25, D-81377 Munich, Germany
strain.
Deleting only the 30 C-terminal amino acids of Yku70p abolishes Yku DNA
binding activity and causes a yku phenotype; telomeres
are shortened, and NHEJ is impaired. Using conditions in which at least
as much mutant protein as full-length protein is normally detectable in
cell extracts, deleting only 25 C-terminal amino acids of Yku70p
results in no measurable effect on DNA binding of the Yku protein, and
the cells are fully proficient for NHEJ. Nevertheless, these cells
display considerably shortened telomeres, and significant amounts of
single-stranded overhangs of the telomeric guanosine-rich strands are
observed. Co-overexpression of this protein with Yku80p could rescue
some but not all of the telomere-related phenotypes. Therefore, the
C-terminal domain in Yku70p defines at least one domain that is
especially involved in telomere maintenance but not in NHEJ.
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant Wi 319/11-3, Project 7, and by Canadian Medical Research Council
Grant MT12616 (to R.J.W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Adolf-Butenandt-Institute for Cell Biology,
University of Munich (LMU), Schillerstr. 42, D-80336
München, Germany.
¶
A chercheur-boursier of the Fonds de la Recherche en
Santé du Québec.
**
To whom correspondence should be addressed: Institut für
Biochemie der Universität München, Feodor-Lynen-Str.
25, D-81377 München, Germany. Tel.: 49-89-2180-6962; Fax:
49-89-2180-6999; E-mail: fmann@lmb.uni-muenchen.de.
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