Structure and evolution of mammalian ribosomal proteins

Wool, Ira G.; Chan, Yuen‐Ling; Glück, Anton

doi:10.1139/o95-101

Cited by 290 publications

(295 citation statements)

References 52 publications

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“…Interestingly, a comparison of the results indicates that the ribosomal proteins of A. thaliana, are modified to a much larger extent, including for some protein families more than 10 different forms (e.g. for L5 and S3, Table 2), compared to the few modifications observed for each ribosomal protein of the other organism analysed (e.g Escherichia coli, (Wittmann-Liebold, 1986); yeast, (Link et al, 1999;Lee et al, 2002); rat, (Wool et al, 1995;Louie et al, 1996); human, (Vladimirov et al, 1996;Odintsova et al, 2003); spinach, and Chlamydomonas reinhardtii, ).…”

Section: Discussionmentioning

confidence: 99%

“…Proteomic analyses of ribosomes from higher eukaryotes have been limited to cytoplasmic ribosomes from rat (Wool et al, 1995;Louie et al, 1996), as well as both the small (Vladimirov et al, 1996) and large subunit (Odintsova et al, 2003) from humans. Although studies have addressed the composition of bacteriallike ribosomes, such as the chloroplast 70S ribosome from Spinacea oleracea and Chlamydomonas reinhardtii , to date, little work has addressed the composition of the higher plant cytoplasmic ribosomes.…”

Section: Introductionmentioning

confidence: 99%

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High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

et al. 2005

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Proteomic studies have addressed the composition of plant chloroplast ribosomes and 70S ribosomes from the unicellular organism Chlamydomonas reinhardtii, but comprehensive characterization of cytoplasmic 80S ribosomes from higher plants has been lacking. We have used two-dimensional gel electrophoresis (2-DE) and mass spectrometry (MS) to analyse the cytoplasmic 80S ribosomes from the model flowering plant Arabidopsis thaliana. Of the 80 ribosomal protein families predicted to comprise the cytoplasmic 80S ribosome, we have confirmed the presence of 61; specifically, 27 (84%) of the small 40S subunit and 34 (71%) of the large 60S subunit. Nearly half (45%) of the ribosomal proteins identified are represented by two or more distinct spots in the 2-DE gel indicating that these proteins are either post-translationally modified or present as different isoforms. Consistently, MS-based protein identification revealed that at least one-third (34%) of the identified ribosomal protein families showed expression of two or more family members. In addition, we have identified a number of non-ribosomal proteins that co-migrate with the plant 80S ribosomes during gradient centrifugation suggesting their possible association with the 80S ribosomes. Among them, RACK1 has recently been proposed to be a ribosome-associated protein that promotes efficient translation in yeast. The study, thus provides the basis for further investigation into the function of the other identified non-ribosomal proteins as well as the biological meaning of the various ribosomal protein isoforms.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

et al. 2005

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“…Given that only proteins from purified ribosomes were analyzed by 2D gel electrophoresis, we consider it unlikely that a suite of minor, nonribosomal proteins of low M r and high IEF would routinely crosslink to RNA and be purified with ribosomes in this analysis. S14 is a cytosolic ribosomal protein; it is a member of Group I when eukaryote ribosomal proteins are classified based on homology to proteins of archae-and eubacteria (Wool et al, 1995). Proteins in Group I have orthologs in eubacteria, archaebacteria, and eukaryotes.…”

Section: Discussionmentioning

confidence: 99%

“…Proteins in Group I have orthologs in eubacteria, archaebacteria, and eukaryotes. Eukaryote ribosomal protein S14 is related to the archaebacterial Halobacterium marismortui S11 and to the eubacterial Escherichia coli S11 (Wool et al, 1995). E. coli ribosomal protein S11 can be in vitro crosslinked to nucleotides 693 to 697 of 16S rRNA using bis-(2-chloroethyl)-methylamine (Greuer et al, 1987) and to nucleotides 702 to 705 of 16S rRNA using S11-methyl p-azidophenyl acetimidate (Osswald et al, 1990); therefore, this protein is in close contact with ribosomal RNA in eubacteria.…”

Section: Discussionmentioning

confidence: 99%

Crosslinking of Ribosomal Proteins to RNA in Maize Ribosomes by UV-B and Its Effects on Translation

Casati

Walbot

2004

Plant Physiology

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Ultraviolet-B (UV-B) photons can cause substantial cellular damage in biomolecules, as is well established for DNA. Because RNA has the same absorption spectrum for UV as DNA, we have investigated damage to this cellular constituent. In maize (Zea mays) leaves, UV-B radiation damages ribosomes by crosslinking cytosolic ribosomal proteins S14, L23a, and L32, and chloroplast ribosomal protein L29 to RNA. Ribosomal damage accumulated during a day of UV-B exposure correlated with a progressive decrease in new protein production; however, de novo synthesis of some ribosomal proteins is increased after 6 h of UV-B exposure. After 16 h without UV-B, damaged ribosomes were eliminated and translation was restored to normal levels. Ribosomal protein S6 and an S6 kinase are phosphorylated during UV-B exposure; these modifications are associated with selective translation of some ribosomal proteins after ribosome damage in mammalian fibroblast cells and may be an adaptation in maize. Neither photosynthesis nor pigment levels were affected significantly by UV-B, demonstrating that the treatment applied is not lethal and that maize leaf physiology readily recovers.The evolution of terrestrial life was made possible by formation of a stratosphere that screens solar UV radiation, absorbing UV-C (,280 nm) and the most energetic UV-B (280-315 nm). Recent depletion of stratospheric ozone by chlorofluorocarbons and other pollutants has increased terrestrial UV-B levels with potentially deleterious consequences for all living organisms and particularly for plant development and physiology (Ballaré et al., 2001;Searles et al., 2001;Paul and Gwynn-Jones, 2003). In response to the inevitable exposure to damaging terrestrial UV-B, plants have evolved UV-induced mechanisms of protection and repair, such as accumulation of UVabsorbing pigments and use of UV-A photons to repair UV-B induced DNA damage (Stapleton and Walbot, 1994;Britt, 1996). Because of its absorption spectrum, DNA is a major target of UV-B radiation (Britt, 1996). This radiation can also damage proteins and lipids directly (Gerhardt et al., 1999); RNA molecules strongly absorb UV-B, but less is known about UV-B mediated damage to this cellular constituent.Experimentally, UV has been extensively used to analyze ribosome structure in vitro, because crosslinks can be introduced at points of close contact between proteins, within ribosomal RNA (rRNA), and between proteins and rRNA, tRNA, or mRNA Noah et al., 2000). Furthermore, in vivo crosslinks are generated in rRNA by UV treatment of bacterial cells (Stiege et al., 1986). In mammalian cells, UV-C and UV-B cause specific damage to the 3#-end of the 28S rRNA activating a response called ribotoxic stress (Iordanov et al., 1997(Iordanov et al., , 1998. Protein synthesis in plant cells is also sensitive to UV-C. Murphy et al. (1973) demonstrated that 254 nm radiation disrupted amino acid incorporation into protein in a wheat germ in vitro synthesis reaction and that the most sensitive target was mRNA. Subsequent studies in cult...

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“…SRP54/Ffh, L11 and S15 ribosomal proteins appear now to define a novel class of helical RNA-binding proteins with a common fold. The conservation of S15, L11 and SRP54 and their RNA ligands among all three phylogenetic kingdoms demonstrates that both the ribosome and SRP, existed before the kingdoms diverged (Wool et al, 1995;Zwieb and Larsen, 1997 and references therein). Their old evolutionary age and the importance of their functional conservation is further strengthened by the comparable and very high primary sequence conservation between the homologous proteins of the three kingdoms.…”

Section: Srp Proteins: Members Of Ancient Nucleic Acid-binding Foldsmentioning

confidence: 99%

New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle

Bui

Strub²

1999

Biological Chemistry

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The signal recognition particle (SRP), a ubiquitous cytoplasmic ribonucleoprotein particle, plays an essential role in promoting co-translational translocation of proteins into the endoplasmic reticulum. Here, we summarise recent progress made in the understanding of two essential SRP functions: the signal recognition function, which ensures the specificity, and the elongation arrest function, which increases the efficiency of translocation. Our discussion is based on functional data as well as on atomic structure information, both of which also support the notion that SRP is a very ancient particle closely related to ribosomes. Based on the significant increase of knowledge that has been accumulating on the structure of elongation factors and on their interactions with the ribosome, we speculate about a possible mechanism of the elongation arrest function.

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Structure and evolution of mammalian ribosomal proteins

Cited by 290 publications

References 52 publications

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome

Crosslinking of Ribosomal Proteins to RNA in Maize Ribosomes by UV-B and Its Effects on Translation

New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle

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