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Implications of N-terminal sequence elements in S. cerevisiae ribosomal protein L5
Södertörn University, School of Life Sciences. Stockholms universitet.
Södertörn University, School of Life Sciences. Stockholms universitet.
Södertörn University, School of Life Sciences.
(English)Manuscript (preprint) (Other academic)
Resource type
Text
Abstract [en]

Yeast ribosomal protein L5 (YrpL5) is an essential 5S rRNA-binding protein that forms the central protuberance of the large ribosomal subunit. Formation of the binary rpL5.5S rRNA complex is a prerequisite for nuclear import of rpL5 and for ribosome assembly. The involvment of the N-terminal sequences of YrpL5 in 5S rRNA interaction and nuclear import was studied by mutagenesis and functional complementation in S. cerevisiae. Furthermore, the ability of YrpL5 orthologous proteins from M. musculus (MrpL5), D. melanogaster (DrpL5) and A. thaliana (ArpL5) were non-functional in yeast cells. Nuclear import of YrpL5 requires conserved sequence elements in the N-terminus. Despite the presence of these elements in ArpL5, this protein was not recognized by the nuclear import machinery in yeast. This failure was probably due to lack of stable complex formation with yeast 5S rRNA.

Keyword [en]
Functional complementation, Mutation analysis, Ribosomal protein L5, nuclear localization, S. cerevisiae
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:sh:diva-30700OAI: oai:DiVA.org:sh-30700DiVA: diva2:951036
Note

Som manuskript i avhandling. As manuscript in dissertation.

Available from: 2009-05-14 Created: 2016-08-05 Last updated: 2016-08-05Bibliographically approved
In thesis
1. Ribosomal proteins L5 and L15: Functional characterisation of important features, in vivo
Open this publication in new window or tab >>Ribosomal proteins L5 and L15: Functional characterisation of important features, in vivo
2009 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Protein synthesis is a highly regulated and energy consuming process, during which a large ribonucleoprotein particle called the ribosome, synthesizes new proteins. The eukaryotic ribosome consists of two unequal subunits called: small and large subunits. Both subunits are composed of ribosomal RNA (rRNA) and ribosomal proteins (r-proteins).

Although rRNAs build the matrix of the ribosome and carries out catalysing of the peptide-bond formation between amino acids, r-proteins also appear to play important structural and functional roles. The primary role of r-proteins is to initiate the correct tertiary fold of rRNA and to organize the overall structure of the ribosome.

In this thesis, I focus on two proteins from the large subunit of the eukaryotic ribosome: r-proteins L5 and L15 from bakers yeast S. cerevisiae. Both r-proteins are essential for ribosome function. Their life cycle is primarily associated with rRNA interactions. As a consequence, the proteins show high sequence homology across the species borders. Furthermore, both L5 and L15 are connected to human diseases, which makes the study their role in ribosome biogenesis and ribosome function important.

By applying random- and site-directed mutagenesis, coupled with functional complementation tests, I aimed to elucidate functionally regions in both proteins, implicated in transport to the cell nucleus, protein-protein interactions and/or rRNA binding. The importance of individual and multiple amino acid exchanges in the primary sequence of rpL5 and rpL15 were studied in vivo. The obtained results show that S. cerevisiae rpL15 was tolerant to amino acid exchanges in the primary sequence, whereas rpL5 was not. Consequently, A. thaliana rpL15 could substitute for the function of wild type rpL15, whereas none of the tested orthologous proteins to rpL5 could substitute yeast rpL5 in vivo. These observations further emphasize the importance of studying r-proteins as separate entities in the ribosome context.

Place, publisher, year, edition, pages
Stockholm: Stockholm University, 2009. 50 p.
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:sh:diva-30701 (URN)978-91-7155-896-1 (ISBN)
Public defence
2009-06-16, MB 503, Södertörns högskola, Alfred Nobels allé 7, 10:00 (English)
Opponent
Supervisors
Available from: 2016-08-05 Created: 2016-08-05 Last updated: 2016-08-05Bibliographically approved

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