Publications by authors named "Lore Koller"

It is our intention to give the reader a short overview of the relationship between apoptosis and senescence in yeast mother cell-specific aging. We are studying yeast as an aging model because we want to learn something of the basic biology of senescence and apoptosis even from a unicellular eukaryotic model system, using its unrivalled ease of genetic analysis. Consequently, we will discuss also some aspects of apoptosis in metazoa and the relevance of yeast apoptosis and aging research for cellular (Hayflick type) and organismic aging of multicellular higher organisms.

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Functional ribosomes synthesize proteins in all living cells and are composed of two labile associated subunits, which are made of rRNA and ribosomal proteins. The rRNA of the small 40S subunit (SSU) of the functional eukaryotic 80S ribosome decodes the mRNA molecule and the large 60S subunit (LSU) rRNA catalyzes protein synthesis. Recent fine structure determinations of the ribosome renewed interest in the role of ribosomal proteins in modulation of the core ribosomal functions.

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An extensive homology search based on the sequence of the yeast protein Brx1p (biogenesis of ribosomes in Xenopus, YOL077c) revealed that it is a member of a superfamily of proteins sharing remarkable sequence similarities. Previous work on Brx1p showed that this protein is involved in the process of ribosome biogenesis [Kaser et al., Biol.

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Article Synopsis
  • The biogenesis of ribosomes and cell surface components are crucial for yeast cell growth, with specific proteins like RpL10p/Grc5p playing key roles in ribosome assembly and maturation.* ! -
  • A study found that the yeast genes SED1, ACS2, and PLB3 interact with RpL10p/Grc5p and its human counterpart, indicating a connection between ribosome function and cellular metabolism.* ! -
  • The protein Sed1p is suggested to have a significant role in translating ribosomes and is involved in cell wall formation, while ACS2 and PLB3 are linked to lipid synthesis and membrane maintenance, respectively.* !
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