LRP1/YHR081W Summary Help

Standard Name LRP1 1
Systematic Name YHR081W
Alias RRP47 2
Feature Type ORF, Verified
Description Nuclear exosome-associated nucleic acid binding protein; involved in RNA processing, surveillance, degradation, tethering, and export; forms a stable heterodimer with Rrp6p and regulates its exonucleolytic activity; rapidly degraded by the proteasome in the absence of Rrp6p; homolog of mammalian nuclear matrix protein C1D involved in regulation of DNA repair and recombination (2, 3, 4, 5, 6, 7 and see Summary Paragraph)
Also known as: YC1D 8
Name Description Like RrP6 1
Chromosomal Location
ChrVIII:267538 to 268092 | ORF Map | GBrowse
Gene Ontology Annotations All LRP1 GO evidence and references
  View Computational GO annotations for LRP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 6 genes
Classical genetics
Large-scale survey
378 total interaction(s) for 261 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 45
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 6
  • Biochemical Activity: 2
  • PCA: 2
  • Reconstituted Complex: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 148
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 103
  • Synthetic Growth Defect: 30
  • Synthetic Lethality: 34

Expression Summary
Length (a.a.) 184
Molecular Weight (Da) 21,045
Isoelectric Point (pI) 10.39
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVIII:267538 to 268092 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..555 267538..268092 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001123

The exosome complex possesses 3'-5' exonuclease and endoribonucleolytic activities that are essential for diverse ribonucleolytic processes in both the nucleus and the cytoplasm (9, 10, 11). The nuclear exosome is associated with the TRAMP complex and is involved in RNA catabolic processes including RNA surveillance (12, 13 and references therein), pre-mRNA turnover (14) and the production of mature 3' ends for snoRNAs, snRNAs and rRNAs (10, 15 and references therein). The cytoplasmic exosome is associated with Ski7p and the SKI complex and is involved in RNA catabolic processes that include both the routine turnover of normal mRNA (16) as well as the degradation of aberrant mRNAs (17 and references therein). The 10-subunit core exosome complex (Csl4p, Rrp4p, Rrp40p, Ski6p, Rrp42p, Rrp43p, Rrp45p, Rrp46p, Mtr3p, Dis3p) is the same in both locations, but the nuclear exosome contains an additional subunit (Rrp6p) and two additional accessory factors (Lrp1p, Mpp6p) (11).

Although the exosome was originally described as a "complex of exonucleases," with multiple subunits proposed to have RNase activity (9), later work has shown that this mechanism is unlikely in yeast. With the exception of Ski6p, none of the yeast subunits that show homology to E. coli RNase PH retain the active site residues seen in the bacterial or archael enzymes. Further research has also demonstrated that most, if not all, detectable enzymatic activity resides in the Dis3p and Rrp6p subunits (18, 19).

Lrp1p is a nucleic acid binding protein associated with the nuclear exosome (2, 4). Lrp1p binds to the exonuclease Rrp6p and also specifically to double-stranded nucleic acid structures (4). lrp1 null mutants are temperature sensitive (8) and are impaired in rRNA, snoRNA, and snRNA precursor processing, as well as mRNA surveillance, degradation, and export, and also in post-transcriptional tethering of genes to the nuclear periphery (2, 5, 3 and references therein). lrp1 mutants are also defective in telomere length maintenance and for repair of DNA damage caused by UV irradiation, non-homologous DNA end joining (NHEJ) and homologous recombination (20, 3, 8). Lrp1p homologs include the S. pombe condensin-associated protein Cti1 and the human nuclear matrix protein C1D (21, 8).

Last updated: 2009-09-09 Contact SGD

References cited on this page View Complete Literature Guide for LRP1
1) Peng WT, et al.  (2003) A panoramic view of yeast noncoding RNA processing. Cell 113(7):919-33
2) Mitchell P, et al.  (2003) Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs. Mol Cell Biol 23(19):6982-92
3) Hieronymus H, et al.  (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62
4) Stead JA, et al.  (2007) The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 35(16):5556-67
5) Vodala S, et al.  (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13
6) Feigenbutz M, et al.  (2013) Assembly of the yeast exoribonuclease rrp6 with its associated cofactor rrp47 occurs in the nucleus and is critical for the controlled expression of rrp47. J Biol Chem 288(22):15959-70
7) Dedic E, et al.  (2014) Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle X-ray scattering. Biochem Biophys Res Commun 450(1):634-40
8) Erdemir T, et al.  (2002) Saccharomyces cerevisiae C1D is implicated in both non-homologous DNA end joining and homologous recombination. Mol Microbiol 46(4):947-57
9) Mitchell P, et al.  (1997) The exosome: a conserved eukaryotic RNA processing complex containing multiple 3'-->5' exoribonucleases. Cell 91(4):457-66
10) van Hoof A, et al.  (2000) Yeast exosome mutants accumulate 3'-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol Cell Biol 20(2):441-52
11) Synowsky SA, et al.  (2009) Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes. J Mol Biol 385(4):1300-13
12) Vanacova S, et al.  (2005) A new yeast poly(A) polymerase complex involved in RNA quality control. PLoS Biol 3(6):e189
13) LaCava J, et al.  (2005) RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 121(5):713-24
14) Bousquet-Antonelli C, et al.  (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75
15) Allmang C, et al.  (2000) Degradation of ribosomal RNA precursors by the exosome. Nucleic Acids Res 28(8):1684-91
16) Jacobs JS, et al.  (1998) The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complex. EMBO J 17(5):1497-506
17) Schaeffer D, et al.  (2008) Determining in vivo activity of the yeast cytoplasmic exosome. Methods Enzymol 448:227-39
18) Liu Q, et al.  (2006) Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127(6):1223-37
19) Dziembowski A, et al.  (2007) A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 14(1):15-22
20) Askree SH, et al.  (2004) A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length. Proc Natl Acad Sci U S A 101(23):8658-63
21) Chen ES, et al.  (2004) Cti1/C1D interacts with condensin SMC hinge and supports the DNA repair function of condensin. Proc Natl Acad Sci U S A 101(21):8078-83