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Protein FULL name:

Ribonucleotide-diphosphate reductase (RNR), small subunit; the RNR complex catalyzes the rate-limiting step in dNTP synthesis and is regulated by DNA replication and DNA damage checkpoint pathways via localization of the small subunits

Rnr4p (Saccharomyces cerevisiae) is product of expression of RNR4 gene.

FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR4 is required for proper folding of RNR2 and assembly with the large subunits.

CATALYTIC ACTIVITY: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.

BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate; Temperature dependence: Optimum temperature is 30 degrees Celsius;

PATHWAY: Genetic information processing; DNA replication.

SUBUNIT: Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3.

INTERACTION: Self; NbExp=1; IntAct=EBI-15251, EBI-15251; P43582:-; NbExp=1; IntAct=EBI-15251, EBI-22766; P22696:ESS1; NbExp=1; IntAct=EBI-15251, EBI-6679; P33203:PRP40; NbExp=1; IntAct=EBI-15251, EBI-701; P09938:RNR2; NbExp=3; IntAct=EBI-15251, EBI-15240; P46995:SET2; NbExp=1; IntAct=EBI-15251, EBI-16985; Q06525:URN1; NbExp=1; IntAct=EBI-15251, EBI-35138;

SUBCELLULAR LOCATION: Nucleus. Note=Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner.

INDUCTION: Induced by DNA-damage.

MISCELLANEOUS: Present with 88884 molecules/cell in log phase SD medium.

MISCELLANEOUS: Lacks 3 iron-binding residues conserved in all other R2 subunits.

SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family.

NCBI GenPept GI number(s): 6321619
Species: Saccharomyces cerevisiae

Links to other databases:

Database ID Link
Uniprot P49723 P49723
PFAM: - P49723 (Link - using uniprot id)
InterPro: - P49723 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -

Protein sequence:

Rnr4p (Saccharomyces cerevisiae) belongs to following protein families:

Title Authors Journal
The nucleotide sequence of Saccharomyces cerevisiae chromosome VII. Tettelin H, Agostoni Carbone ML, Albermann K, Albers M, Arroyo J, Backes U, Barreiros T, Bertani I, Bjourson AJ, Bruckner M, Bruschi CV, Carignani G, Castagnoli L, Cerdan E, Clemente ML, Coblenz A, Coglievina M, Coissac E, Defoor E, Del Bino S, Delius H, Delneri D, de Wergifosse P, Dujon B, Kleine K, et al. Nature May 1, 1997
Rnr4p, a novel ribonucleotide reductase small-subunit protein. Wang PJ, Chabes A, Casagrande R, Tian XC, Thelander L, Huffaker TC Mol Cell Biol Oct. 1, 1997
Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly. Nguyen HH, Ge J, Perlstein DL, Stubbe J Proc Natl Acad Sci U S A Oct. 26, 1999
Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit. Chabes A, Domkin V, Larsson G, Liu A, Graslund A, Wijmenga S, Thelander L Proc Natl Acad Sci U S A March 14, 2000
Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC Proc Natl Acad Sci U S A Aug. 28, 2001
Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways. Yao R, Zhang Z, An X, Bucci B, Perlstein DL, Stubbe J, Huang M Proc Natl Acad Sci U S A May 27, 2003
Global analysis of protein expression in yeast. Ghaemmaghami S, Huh WK, Bower K, Howson RW, Belle A, Dephoure N, O'Shea EK, Weissman JS Nature Oct. 16, 2003
Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers. Sommerhalter M, Voegtli WC, Perlstein DL, Ge J, Stubbe J, Rosenzweig AC Biochemistry June 22, 2004
Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway. Gruhler A, Olsen JV, Mohammed S, Mortensen P, Faergeman NJ, Mann M, Jensen ON Mol Cell Proteomics March 1, 2005
Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry. Chi A, Huttenhower C, Geer LY, Coon JJ, Syka JE, Bai DL, Shabanowitz J, Burke DJ, Troyanskaya OG, Hunt DF Proc Natl Acad Sci U S A Jan. 13, 2007
Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Hu Y, Rolfs A, Bhullar B, Murthy TV, Zhu C, Berger MF, Camargo AA, Kelley F, McCarron S, Jepson D, Richardson A, Raphael J, Moreira D, Taycher E, Zuo D, Mohr S, Kane MF, Williamson J, Simpson A, Bulyk ML, Harlow E, Marsischky G, Kolodner RD, LaBaer J Genome Res April 1, 2007
Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Smolka MB, Albuquerque CP, Chen SH, Zhou H Proc Natl Acad Sci U S A June 19, 2007
A multidimensional chromatography technology for in-depth phosphoproteome analysis. Albuquerque CP, Smolka MB, Payne SH, Bafna V, Eng J, Zhou H Mol Cell Proteomics July 1, 2008

Last modification of this entry: Oct. 6, 2010.

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