RIP1/YEL024W Summary Help

Standard Name RIP1 1
Systematic Name YEL024W
Feature Type ORF, Verified
Description Ubiquinol-cytochrome-c reductase; a Rieske iron-sulfur protein of the mitochondrial cytochrome bc1 complex; transfers electrons from ubiquinol to cytochrome c1 during respiration; during import, Rip1p is first imported into the mitochondrial matrix where it is processed, acquires its Fe-S cluster, and is folded, then is translocated into the inner membrane by the action of a homo-oligomer of Bcs1p, and finally is delivered by Bcs1p to Complex III for assembly (2, 3, 4, 5 and see Summary Paragraph)
Name Description Rieske Iron-sulfur Protein 1
Chromosomal Location
ChrV:107260 to 107907 | ORF Map | GBrowse
Gene Ontology Annotations All RIP1 GO evidence and references
  View Computational GO annotations for RIP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 7 genes
Classical genetics
Large-scale survey
107 total interaction(s) for 92 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 6
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 17
  • Co-fractionation: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 2

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 58
  • Phenotypic Suppression: 1
  • Positive Genetic: 7
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 11

Expression Summary
Length (a.a.) 215
Molecular Weight (Da) 23,365
Isoelectric Point (pI) 8.07
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:107260 to 107907 | ORF Map | GBrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..648 107260..107907 1996-07-31 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000750

The cytochrome bc1 complex (also known as ubiquinol:cytochrome c oxidoreductase, ubiquinol:ferricytochrome c oxidoreductase, and respiratory complex III) is a highly conserved enzyme of the mitochondrial respiratory chain (reviewed in 6). In S. cerevisiae it consists of three catalytic subunits, Cobp, Rip1p, and Cyt1p, plus seven additional subunits: Cor1p, Qcr2p, Qcr6p, Qcr7p, Qcr8p, Qcr9p, and Qcr10p (6, 7). The crystal structure of the complex shows that two functional units, each containing these ten subunits, associate with each other in the mitochondrial inner membrane (8). Assembly of a functional complex requires two proteins, Cbp3p and Cbp4p, that are not components of the complex but may associate with it during assembly (9). It also requires Bcs1p, an AAA-family ATPase that interacts with a precursor of the complex to mediate incorporation of the Rip1p and Qcr10p subunits (10). The mechanism of energy transfer by the complex, known as the protonmotive Q cycle, has been studied in detail (reviewed in 6). The net result of the Q cycle is the stepwise transfer of an electron through the complex from ubiquinol to cytochrome c (Cyc1p), coupled with the translocation of a proton across the mitochondrial inner membrane (6). The function of the cytochrome bc1 complex is essential to the energy-generating process of oxidative phosphorylation, which is carried out by the enzyme complexes of the mitochondrial respiratory chain.

Rip1p, known as the Rieske iron-sulfur protein after the biochemist J.S. Rieske who first identified it, is one of the catalytic subunits of the cytochrome bc1 complex and is essential for activity of the complex and for respiratory growth (1, 2, 11). It contains an iron-sulfur cluster and is involved in electron transport from ubiquinol to cytochrome c1 (Cyt1p); a conformational change in the catalytic domain is believed to occur during this process, facilitated by a flexible linker region (6, 12). RIP1 is conserved across both prokaryotes and eukaryotes (13); its human homolog is UQCRFS1 (OMIM).

Last updated: 2007-07-26 Contact SGD

References cited on this page View Complete Literature Guide for RIP1
1) Beckmann JD, et al.  (1987) Isolation and characterization of the nuclear gene encoding the Rieske iron-sulfur protein (RIP1) from Saccharomyces cerevisiae. J Biol Chem 262(18):8901-9
2) Ljungdahl PO, et al.  (1989) Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. II. Biochemical characterization of temperature-sensitive RIP1- mutations. J Biol Chem 264(7):3723-31
3) Graham LA, et al.  (1993) Mutational analysis of assembly and function of the iron-sulfur protein of the cytochrome bc1 complex in Saccharomyces cerevisiae. J Bioenerg Biomembr 25(3):245-57
4) Obungu VH, et al.  (1998) The role of charged amino acids in the alpha1-beta4 loop of the iron-sulfur protein of the cytochrome bc1 complex of yeast mitochondria. J Biol Chem 273(19):11917-22
5) Wagener N, et al.  (2011) A pathway of protein translocation in mitochondria mediated by the AAA-ATPase Bcs1. Mol Cell 44(2):191-202
6) Hunte C, et al.  (2003) Protonmotive pathways and mechanisms in the cytochrome bc1 complex. FEBS Lett 545(1):39-46
7) Brandt U, et al.  (1994) Isolation and characterization of QCR10, the nuclear gene encoding the 8.5-kDa subunit 10 of the Saccharomyces cerevisiae cytochrome bc1 complex. J Biol Chem 269(17):12947-53
8) Hunte C, et al.  (2000) Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Structure 8(6):669-84
9) Kronekova Z and Rodel G  (2005) Organization of assembly factors Cbp3p and Cbp4p and their effect on bc(1) complex assembly in Saccharomyces cerevisiae. Curr Genet 47(4):203-12
10) Cruciat CM, et al.  (1999) Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex. EMBO J 18(19):5226-33
11) Beckmann JD, et al.  (1989) Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. I. Construction of a RIP1 deletion strain and isolation of temperature-sensitive mutants. J Biol Chem 264(7):3713-22
12) Ghosh M, et al.  (2001) Substituting leucine for alanine-86 in the tether region of the iron-sulfur protein of the cytochrome bc1 complex affects the mobility of the [2Fe2S] domain. Biochemistry 40(2):327-35
13) Trumpower BL  (1990) Cytochrome bc1 complexes of microorganisms. Microbiol Rev 54(2):101-29