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Functional and physical interactions of Krr1p, a Saccharomyces cerevisiae nucleolar protein

100%

Gromadka R., Karkusiewicz I., Rempola B., Rytka J.

Acta Biochimica Polonica

2004

tom 51

nr 1

The Krr1 protein of Saccharomyces cerevisiae is involved in processing of pre-rRNA and assembly of pre-ribosomal 40S subunits. To further investigate the function of Krr1p we constructed a conditional cold sensitive mutant krrl-21, and isolated seven genes from Schizosaccharomyces pombe whose products suppressed the cold sensitive phenotype of krrl-21 cells. Among the multicopy suppressors we found genes coding for translation elongation factor EF-1a, a putative ribose methyltransferase and five genes encoding ribosomal proteins. Using the tandem affinity purification (TAP) method we identified thirteen S. cerevisiae ribosomal proteins interacting with Krr1p. Taken together, these results indicate that Krr1p interacts functionally as well as physically with ribosomal proteins. Northern blot analysis revealed that changes in the level of krrl-21 mRNA were accompanied by similar changes in the level of mRNAs of genes encoding ribosomal proteins. Thus, Krr1p and the genes encoding ribosomal proteins it interacts with seem to be coordinately regulated at the level of transcription.

The GTPase domain of Galphao contributes to the functional interactions of Galphao with the promyelocytic leukemia zinc finger protein

80%

Won J. H., Ghil S. H.

Cellular and Molecular Biology Letters

2009

tom 14

nr 1

46-56

Go, one of the most abundant heterotrimeric G proteins in the brain, is classified as a member of the Gi/Go family based on its homology to Gi proteins. Recently, we identified promyelocytic leukemia zinc finger protein (PLZF) as a candidate downstream effector for the alpha subunit of Go (Gαo). Activated Gαo interacts with PLZF and augments its function as a repressor of transcription and cell growth. G protein-coupled receptor-mediated Gαo activation also enhanced PLZF function. In this study, we determined that the GTPase domain of Gαo contributes to Gαo:PLZF interaction. We also showed that the Gαo GTPase domain is important in modulating the function of PLZF. This data indicates that the GTPase domain of Gαo may be necessary for the functional interaction of Gαo with PLZF.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Cellular and Molecular Biology Letters

1 Ghil S. H.

1 Gromadka R.

1 Karkusiewicz I.

1 Rempola B.

1 Rytka J.

1 Won J. H.

1 2009

1 2004

Wyniki wyszukiwania

Functional and physical interactions of Krr1p, a Saccharomyces cerevisiae nucleolar protein

The GTPase domain of Galphao contributes to the functional interactions of Galphao with the promyelocytic leukemia zinc finger protein