Modification of yeast ribosomal proteins. Methylation

Kruiswijk, T.; Kunst, A; Planta, Rudi J.; Mager, Willem H.

doi:10.1042/bj1750221

Cited by 39 publications

(31 citation statements)

References 21 publications

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“…YL1 (L3) was detected only by Cannon et al [ 5 ] . In the small subunit, Kruiswijk et al [7] detected, as we found, protein YS28 (S32) as the most significantly methylated. On the other hand, Hernandez et al of YS5 (S4).…”

Section: Identification Of the Ribosomal Proteins Methylated In Vivosupporting

confidence: 51%

“…Taking into account the fact that half of the protein radioactivity was in basic amino acids, we can estimate that the large subunit contains about 10 methyl groups in protein while the small contains only a few (2 -4), This estimation is much higher than that of Kruiswijk el a]. [7], who used a double-labelling method and estimated, indirectly, that the large and small subunits contained 0.29 and 0.25 methyl group respectively.…”

Section: Results a N D Discussionmentioning

confidence: 76%

“…It is clear that Cannon et al [5] as well as Kruiswijk et al [7] have detected methylation of YL23 (L15).…”

Section: Identification Of the Ribosomal Proteins Methylated In Vivomentioning

confidence: 99%

“…On the other hand, Hernandez et al of YS5 (S4). a protein not found lo be methylated by Kruiswijk et al [7].…”

Section: Identification Of the Ribosomal Proteins Methylated In Vivomentioning

confidence: 99%

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Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

et al. 1984

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The occurrence of methylated proteins in the ribosomes of Saccharomyces cerevisiue was investigated by tracing the transfer of radioactive methyl groups from S-adenosyl methionine, taken up by growing cells, into the protein moiety of ribosomes. It was estimated that the large subunit contained about 10 protein-bound methyl groups distributed mainly among proteins YL23, YL32 and YL1. The small subunit contained at most 2 -4 methyl groups in proteins. Methyl groups could be transferred in vifro to proteins YL23 and YL32 in extracts from cultures of an Sadenosyl methionine auxotroph deprived of the methyl-group donor. In the most heavily methylated proteins the methylated amino acids formed in vitro were the same as those found in vivo (monomethyllysine and dimethyllysine in YL32; dimethyl and trimethyllysine in YL23). It is concluded that the enzymatic reaction in vitro faithfully saturates with methyl groups the target amino acids which are normally fully methylated in zjiz>o.

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Section: Identification Of the Ribosomal Proteins Methylated In Vivosupporting

confidence: 51%

Section: Results a N D Discussionmentioning

confidence: 76%

“…It is clear that Cannon et al [5] as well as Kruiswijk et al [7] have detected methylation of YL23 (L15).…”

Section: Identification Of the Ribosomal Proteins Methylated In Vivomentioning

confidence: 99%

“…On the other hand, Hernandez et al of YS5 (S4). a protein not found lo be methylated by Kruiswijk et al [7].…”

Section: Identification Of the Ribosomal Proteins Methylated In Vivomentioning

confidence: 99%

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Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

et al. 1984

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“…There are currently 137 established ribosomal protein genes in Saccharomyces cerevisiae, which encode 79 unique ribosomal proteins (46 large subunit and 33 small subunit) (8). The physical and biochemical characterization of yeast ribosomes has been complicated not only by the large number of proteins involved, and their highly basic amino acid content, but also by the presence of modifications, often in combination, including N-terminal processing and acetylation (9), methylation (21,22), and phosphorylation (23,24).…”

mentioning

confidence: 99%

Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR

Lee

Berger

Martinović

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

182

133

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Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry coupled with capillary reverse-phase liquid chromatography was used to characterize intact proteins from the large subunit of the yeast ribosome. High mass measurement accuracy, achieved by ''mass locking'' with an internal standard from a dual electrospray ionization source, allowed identification of ribosomal proteins. Analyses of the intact proteins revealed information on cotranslational and posttranslational modifications of the ribosomal proteins that included loss of the initiating methionine, acetylation, methylation, and proteolytic maturation. High-resolution separations permitted differentiation of protein isoforms having high structural similarity as well as proteins from their modified forms, facilitating unequivocal assignments. The study identified 42 of the 43 core large ribosomal subunit proteins and 58 (of 64 possible) core large subunit protein isoforms having unique masses in a single analysis. These results demonstrate the basis for the high-throughput analyses of complex mixtures of intact proteins, which we believe will be an important complement to other approaches for defining protein modifications and their changes resulting from physiological processes or environmental perturbations.M ass spectrometry has evolved into a powerful tool for analyzing biomolecules because of the development of matrix-assisted laser desorption ionization (1, 2) and electrospray ionization (ESI) (3) and advances in both mass analyzers and data processing capabilities. With these ionization methods, which are amenable to megadalton-size molecules, the broadly useful detection and characterization of biopolymers by mass spectrometric methods are feasible. For example, MS has become a preferred analytical tool for proteome analyses, in which dynamic populations of proteins are identified and quantified. Proteins are now routinely identified by mass spectrometric and tandem mass spectrometric analysis of proteolytic digests of individual protein spots on two-dimensional (2D) PAGE (4). However, the intact protein level analyses of complex protein mixtures, while potentially providing complementary and direct information for protein identification, have been a much greater experimental challenge and only rarely attempted (5, 6).Many pivotal cellular processes are not carried out by individual proteins, but rather by large protein-protein complexes and protein-nucleic acid complexes. The analyses of such complexes have been greatly expanded by improvements in both biological separations and MS. One of the more complicated protein complexes yet studied by MS is the cytosolic ribosome complex. Efforts to define the protein composition (7, 8), modifications (9), and subunit interactions (10) of ribosomes generally have mirrored the development of biomolecular analysis techniques and experimental approaches for the study of noncovalent protein complexes.Ribosomes are the canonical example of ribonucleoprotein complexes in both prokaryot...

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Post-Translational Methylations of Ribosomal Proteins

Alix

1988

Advances in Post-Translational Modifications of Proteins and Aging

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Modification of yeast ribosomal proteins. Methylation

Cited by 39 publications

References 21 publications

Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

Methylated proteins and amino acids in the ribosomes of Saccharomyces cerevisiae

Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR

Post-Translational Methylations of Ribosomal Proteins

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