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Ribosome assembly and function – are there alternative roles for ribosomal proteins?

Ribosome assembly and function – are there alternative roles for ribosomal proteins?

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An essay for the 2011 Undergraduate Awards (Ireland) Competition by Cáit Ní Chorcora.
An essay for the 2011 Undergraduate Awards (Ireland) Competition by Cáit Ní Chorcora.

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Published by: Undergraduate Awards on Aug 31, 2012
Copyright:Attribution Non-commercial


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Ribosome assembly and function – are there alternative roles for ribosomalproteins?
It has long been known that the ribosome is the protein factory of the cell, performingthe last step in the gene expression pathway, translating the information contained inmRNA to produce protein molecules (Liljas, 2004). Ribosomes are found in all cellsand in many different cellular compartments. The ribosome is composed of ribosomalRNA (rRNA) and protein molecules which combine to form the large and a smallribosomal subunit. Ribosomal RNA is not translated but forms the core of theribosomal subunits and interacts extensively with the ribosomal proteins, small proteins with a molecular weight of less then 20kDa (Liljas, 2004).The process of ribosomal synthesis and assembly is vital to the functioning of the cell.The first part of this essay will examine recent literature suggesting that the break-down of this process can have lethal effects on the cell (Belin et al., 2009). Indeed, thedysregulation of ribosome production can have wide-ranging and devastating effectson cellular biochemistry. Ribosomal proteins are known to be central to ribosomal biogenesis. The huge variety of effects the breakdown of this process can have on thecell has led scientists to suspect that these proteins may have additional extra-ribosomal functions in the cell (Warner & McIntosh, 2009). Investigations into thisare discussed in the second part of this review.The process of translation involves the conversion of the information contained inchromosomal DNA into messenger RNA (mRNA). The 3-nucleotide codon of mRNAis then translated into one of the 20 amino acids that make up proteins. The expression1
of an organism’s genetic information in DNA through protein production is critical toall life; all organisms have ribosomes for synthesis of proteins (Liljas, 2004).Translation begins once the DNA nucleotide sequence has been transcribed to mRNA.The mRNA moves to the small ribosomal subunit where it specifically binds to thestart signal, an initiator codon in the P-site of the ribosome small subunit. An initiator transfer RNA (t-RNA) molecule also recognises this start codon and when bothmRNA and initiator tRNA are bound to the P-site the large subunit can bind andtranslation can begin (Liljas, 2004).Since all organisms show this conserved method of protein synthesis, the ribosomewas traditionally thought to have remained unchanged over 3 billion years of evolution (McIntosh et al., 2007). The intricate structure of the ribosomal RNA(rRNA) with their associated proteins is only beginning to be understood and it is becoming clear that the ribosome is far more versatile then originally thought. It wasonly in 2000 that Ban et al. determined the crystal structure of the large ribosomalsubunit from the eukaryotic archaeon
 Haloarcula marismortui
. RNA was also foundto interact with the proteins of the ribosomal subunit, producing a stabilising effect onthe large nucleic acid (RNA) component of the ribosome (Ban et al., 2000).Ribosomal assembly is highly a conserved and co-ordinated process. More then 100accessory proteins are required for proper processing of ribosomal RNAs andribosome assembly (Fatica and Tollervey, 2002). RNA binding proteins play animportant part in this process in eukaryotes and are involved in controlling a varietyof cellular activites. These include RNA maturation, trafficking, stability and2
translational control of mRNA as well as having roles in ribosomal biogenesis(Kressler et al., 1999).Regulation of a cells growth and division is dependant on the control of synthesis of new ribosomes. The process of ribosome biogenesis is energetically costly to the celland so must be tightly regulated in response to changing environmental conditions(Warner at al., 2001). Ribosome biogenesis is tightly controlled in response to a widevariety of intra and extra cellular stimuli. The target of rapamycin (TOR) signaling pathway, which regulates ribosome and protein synthesis, is known to beevolutionarily conserved and has remained unchanged throughout evolution (Chédinet al., 2007). This further indicates the importance of the process of ribosome production.Ribosome synthesis involves the coordinated activity of the three forms of RNA polymerase to produce the various constituents needed for ribosome construction(Chédin et al., 2007). Ribosome biogenesis involves both transcriptional and post-transcriptional steps to produce ribosomes functional in protein synthesis (Melese &Zue, 1995). All eukaryotic ribosomes are made up of four different ribosomal RNAssynthesized by RNA polymerase I and RNA pol III, these associate with 80 ribosomal proteins to form the small (40S) and large (60S) ribosomal subunits (Belin et al.,2009). Importantly, these rRNAs are first synthesized as precursor rRNA and aresubject to considerable co- and post transcriptional processing to produce mature,functional rRNA (Rouquette et al., 2005).3

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