SUMMARY PARAGRAPH for RPP1B
About yeast ribosomes...
Ribosomes are highly conserved large ribonucleoprotein (RNP) particles, consisting in yeast of a large 60S subunit and a small 40S subunit, that perform protein synthesis. Yeast ribosomes contain one copy each of four ribosomal RNAs (5S, 5.8S, 18S, and 25S; produced in two separate transcripts encoded within the rDNA repeat present as hundreds of copies on Chromosome 12) and 78 different ribosomal proteins (r-proteins), which are encoded by 137 different genes scattered about the genome, 59 of which are duplicated (5). The 60S subunit contains 42 proteins and three RNA molecules: 25S RNA of 3392 nt, hydrogen bonded to the 5.8S RNA of 158 nt and associated with the 5S RNA of 121 nt. The 40S subunit has a single 18S RNA of 1798 nt and 32 proteins (6). All yeast ribosomal proteins have a mammalian homolog (1).
In a rapidly growing yeast cell, 60% of total transcription is devoted to ribosomal RNA, and 50% of RNA polymerase II transcription and 90% of mRNA splicing are devoted to the production of mRNAs for r-proteins. Coordinate regulation of the rRNA genes and 137 r-protein genes is affected by nutritional cues and a number of signal transduction pathways that can abruptly induce or silence the ribosomal genes, whose transcripts have naturally short lifetimes, leading to major implications for the expression of other genes as well (7, 8, 9). The expression of some r-protein genes is influenced by Abf1p (10), and most are directly induced by binding of Rap1p to their promoters, which excludes nucleosomes and recruits Fhl1p and Ifh1p to drive transcription (11).
Ribosome assembly is a complex process, with different steps occurring in different parts of the cell. Ribosomal protein genes are transcribed in the nucleus, and the mRNA is transported to the cytoplasm for translation. The newly synthesized r-proteins then enter the nucleus and associate in the nucleolus with the two rRNA transcripts, one of which is methylated and pseudouridylated (view sites of modifications), and then cleaved into three individual rRNAs (18S, 5.8S, and 25S) as part of the assembly process (5). Separate ribosomal subunits are then transported from the nucleolus to the cytoplasm where they assemble into mature ribosomes before functioning in translation (12, 13). Blockage of subunit assembly, such as due to inhibition of rRNA synthesis or processing, results in degradation of newly synthesized r-proteins (14, 13). (For more information on the early steps of rRNA processing and small ribosomal subunit assembly, see the summary paragraph for the U3 snoRNA, encoded by snR17A and snR17B.)
About ribosomal stalk proteins ...
The ribosome has a lateral protuberance called the stalk that interacts with elongation factor EF2 (Eft1p, Eft2p) (15). The stalk is formed by five acidic proteins organized as a pentameric complex (P0-[P1A-P2B]/[P1B-P2A]), with P0 acting as an anchor linking the stalk to the ribosome and directly interacting with the large rRNA GTPase-associated domain (16, 17). P0 is encoded by RPP0, P1 by RPP1A and RPP1B, and P2 by RPP2A and RPP2B. The P2 proteins are on the periphery of the stalk complex, shielding the P1 proteins, which interact with P0 (18). P0 is a scaffolding protein with two short amino acid regions located at positions 199-230 and 231-258 that are responsible for independent binding of two heterodimers, P1A-P2B and P1B-P2A, respectively (16, 17). The P1A-P2B heterodimer is the key element in stalk formation, and the P1B-P2A heterodimer has been implicated in regulation of stalk function (16). The yeast P0, P1, and P2 proteins are homologous to the mammalian P0, P1, and P2 proteins (1).
Last updated: 2007-02-15