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Content available remote YOR129c, a new element interacting with Cnm67p, a component of the spindle pole body of Saccharomyces cerevisiae.
100%
Wysocka M. , Białkowska A. , Miciałkiewicz A. , Kurlandzka A.
Acta Biochimica Polonica
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2003
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tom 50
|
nr 3
883-890
EN
The Saccharomyces cerevisiae spindle pole body (SPB) consists of numerous proteins forming the outer, inner and central plaques. The protein Cnm67 is an important component of the outer plaque. The C-terminus of this protein contains a determinant important for its SPB localization. We identified a protein encoded by YOR129c which interacts with this C-terminus in the two-hybrid system. YOR129c and CNM67 exhibit weak genetic interaction. The double deletion strain yor129cΔ cnm67Δ exhibits moderately increased resistance to 0.1 M LiCl and hygromycin B compared with the cnm67Δ single mutant. We propose that the YOR129c protein is an accessory factor associated with the cytoplasmic face of SPB and plays a role in cation homeostasis and/or multidrug resistance.
2
YOR129c, a new element interacting with Cnm67p, a component of the spindle pole body of Saccharomyces cerevisiae
86%
Wysocka M. , Bialkowska A. , Micialkiewicz A. , Kurlandzka A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 3
EN
The Saccharomyces cerevisiae spindle pole body (SPB) consists of numerous pro­teins forming the outer, inner and central plaques. The protein Cnm67 is an important component of the outer plaque. The C-terminus of this protein contains a determinant important for its SPB localization. We identified a protein encoded by YOR129c which interacts with this C-terminus in the two-hybrid system. YOR129c and CNM67 exhibit weak genetic interaction. The double deletion strain yor129cΔ cnm67Δ exhibits mod­erately increased resistance to 0.1 M LiCl and hygromycin B compared with the cnm67Δ single mutant. We propose that the YOR129c protein is an accessory factor associated with the cytoplasmic face of SPB and plays a role in cation homeostasis and/or multidrug resistance.
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