RPS14A/YCR031C Summary Help

Standard Name RPS14A
Systematic Name YCR031C
Alias CRY1 1 , 2 , RPL59
Feature Type ORF, Verified
Description Protein component of the small (40S) ribosomal subunit; required for ribosome assembly and 20S pre-rRNA processing; mutations confer cryptopleurine resistance; homologous to mammalian ribosomal protein S14 and bacterial S11; RPS14A has a paralog, RPS14B, that arose from the whole genome duplication (3, 4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description Ribosomal Protein of the Small subunit
Gene Product Alias S11 8 , S14A 9 , rp59A 9
Chromosomal Location
ChrIII:178220 to 177500 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 26 cM
Gene Ontology Annotations All RPS14A GO evidence and references
  View Computational GO annotations for RPS14A
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 9 genes
Resources
Classical genetics
null
unspecified
Large-scale survey
gain of function
null
overexpression
reduction of function
Resources
150 total interaction(s) for 139 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 96
  • Affinity Capture-RNA: 8
  • Affinity Capture-Western: 3
  • Co-purification: 2
  • Protein-peptide: 5
  • Reconstituted Complex: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 17
  • Positive Genetic: 8
  • Synthetic Growth Defect: 5
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 137
Molecular Weight (Da) 14,537
Isoelectric Point (pI) 11.43
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIII:178220 to 177500 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: 26 cM
Last Update Coordinates: 2011-02-03 | Sequence: 2000-09-13
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..7 178220..178214 2011-02-03 2000-09-13
Intron 8..314 178213..177907 2011-02-03 2000-09-13
CDS 315..721 177906..177500 2011-02-03 2000-09-13
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000627
SUMMARY PARAGRAPH for RPS14A

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 79 different ribosomal proteins (r-proteins), which are encoded by 137 different genes scattered about the genome, 59 of which are duplicated (10, 8). The 60S subunit contains 46 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 33 proteins (11, 8). All yeast ribosomal proteins have a mammalian homolog (12).

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 (13, 14, 15). The expression of some r-protein genes is influenced by Abf1p (16), and most are directly induced by binding of Rap1p to their promoters, which excludes nucleosomes and recruits Fhl1p and Ifh1p to drive transcription (17).

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 (10). Separate ribosomal subunits are then transported from the nucleolus to the cytoplasm where they assemble into mature ribosomes before functioning in translation (4, 18). Blockage of subunit assembly, such as due to inhibition of rRNA synthesis or processing, results in degradation of newly synthesized r-proteins (19, 18). (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.)

Last updated: 2014-06-20 Contact SGD

References cited on this page View Complete Literature Guide for RPS14A
1) Larkin JC and Woolford JL Jr  (1983) Molecular cloning and analysis of the CRY1 gene: a yeast ribosomal protein gene. Nucleic Acids Res 11(2):403-20
2) Himmelfarb HJ, et al.  (1984) Molecular cloning and biosynthetic regulation of cry1 gene of Saccharomyces cerevisiae. Mol Gen Genet 195(3):500-6
3) Larkin JC, et al.  (1987) Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene. Mol Cell Biol 7(5):1764-75
4) Moritz M, et al.  (1990) Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly. J Cell Biol 111(6 Pt 1):2261-74
5) Lecompte O, et al.  (2002) Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale. Nucleic Acids Res 30(24):5382-90
6) Jakovljevic J, et al.  (2004) The carboxy-terminal extension of yeast ribosomal protein S14 is necessary for maturation of 43S preribosomes. Mol Cell 14(3):331-42
7) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
8) Jenner L, et al.  (2012) Crystal structure of the 80S yeast ribosome. Curr Opin Struct Biol 22(6):759-67
9) Planta RJ and Mager WH  (1998) The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast 14(5):471-7
10) Venema J and Tollervey D  (1999) Ribosome synthesis in Saccharomyces cerevisiae. Annu Rev Genet 33:261-311
11) Verschoor A, et al.  (1998) Three-dimensional structure of the yeast ribosome. Nucleic Acids Res 26(2):655-61
12) Mager WH, et al.  (1997) A new nomenclature for the cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Nucleic Acids Res 25(24):4872-5
13) Li B, et al.  (1999) Transcriptional elements involved in the repression of ribosomal protein synthesis. Mol Cell Biol 19(8):5393-404
14) Zhao Y, et al.  (2003) Autoregulation in the biosynthesis of ribosomes. Mol Cell Biol 23(2):699-707
15) Warner JR  (1999) The economics of ribosome biosynthesis in yeast. Trends Biochem Sci 24(11):437-40
16) Mager WH and Planta RJ  (1990) Multifunctional DNA-binding proteins mediate concerted transcription activation of yeast ribosomal protein genes. Biochim Biophys Acta 1050(1-3):351-5
17) Zhao Y, et al.  (2006) Fine-structure analysis of ribosomal protein gene transcription. Mol Cell Biol 26(13):4853-62
18) Milgrom E, et al.  (2007) Loss of vacuolar proton-translocating ATPase activity in yeast results in chronic oxidative stress. J Biol Chem 282(10):7125-36
19) Wang S, et al.  (2007) Influence of Substrate Conformation on the Deglycosylation of Ribonuclease B by Recombinant Yeast Peptide:N-glycanase. Acta Biochim Biophys Sin (Shanghai) 39(1):8-14