HSP60/YLR259C Summary

HSP60/YLR259C Summary

Standard Name	HSP60 1
Systematic Name	YLR259C
Alias	CPN60 2 , MIF4 3 , MNA2 4 , 5
Feature Type	ORF, Verified
Description	Tetradecameric mitochondrial chaperonin required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; phosphorylated (1, 3, 6, 7, 8, 9)
Name Description	Heat Shock Protein 1, 10

Chromosomal Location	ChrXII:665002 to 663284 \| ORF Map \| GBrowse
	Note: this feature is encoded on the Crick strand.

Gene Ontology Annotations All HSP60 GO evidence and references

	View Computational GO annotations for HSP60
Molecular Function
Manually curated	ATPase activity (IDA) chaperone binding (IPI) DNA replication origin binding (IDA) single-stranded DNA binding (IDA) unfolded protein binding (IMP)
Biological Process
Manually curated	'de novo' protein folding (IMP) chaperone-mediated protein complex assembly (IMP) protein import into mitochondrial intermembrane space (IMP) protein maturation (IMP) protein refolding (IDA, IMP) protein stabilization (IMP)
Cellular Component
Manually curated	mitochondrial nucleoid (IDA) mitochondrion (IDA)
High-throughput	mitochondrion (IDA)

Mutant phenotypes All HSP60 Phenotype evidence and references

Classical genetics
conditional	inviable mitochondrial rho- mutation frequency: increased Hsp60p activity: absent vegetative growth: decreased rate
null	inviable
Large-scale survey
null	haploinsufficient inviable vegetative growth: decreased
reduction of function	competitive fitness: decreased
Resources	PROPHECY \| SCMD \| ScreenTroll \| Yeast Fitness Database

interactions All HSP60 Interaction evidence and references

	145 total interaction(s) for 132 unique genes/features.
Physical Interactions	Affinity Capture-MS: 60 Affinity Capture-RNA: 4 Affinity Capture-Western: 1 Biochemical Activity: 3 Co-fractionation: 1 Co-purification: 2 Reconstituted Complex: 7 Two-hybrid: 1
Genetic Interactions	Negative Genetic: 63 Synthetic Growth Defect: 1 Synthetic Lethality: 2
Resources	BioGRID \| BOND \| BioPIXIE \| CYC2008 (complexes) \| Complexome \| DIP \| DRYGIN \| GeneMANIA \| InterologFinder \| YeastRC Mass Spec

Expression Summary


Resources	Expression Summary \| Cell cycle and metabolic oscillation \| Cell cycle transcript profile \| Cyclebase \| Genevestigator \| GermOnline \| SPELL \| YMGV \| YeastFunc

Protein Information All HSP60 Protein evidence and references

Localization	YeastRC \| YPL+ \| YeastGFP
Phosphorylation	PhosphoGRID \| PhosphoPep Database
Structure	GPMDB \| SCOP \| YeastRC
Homologs	Ashbya (AGD) \| AspGD Homologs \| CGD Homologs \| CandidaDB Homologs \| Fungal Orthogroups Repository \| P-POD \| PDB Homologs \| PhylomeDB \| YGOB \| YOGY

sequence information

ChrXII:665002 to 663284 | |

Note: this feature is encoded on the Crick strand.

SGD ORF map

Last Update

Coordinates: 2011-02-03 | Sequence: 1996-07-31

Subfeature details

	Relative Coordinates	Chromosomal Coordinates	Most Recent Updates
	Relative Coordinates	Chromosomal Coordinates	Coordinates	Sequence
CDS	1..1719	665002..663284	2011-02-03	1996-07-31

Retrieve sequences

Analyze Sequence

S288C only	BLASTP \| ATCC/WashU Clones \| BLASTN \| Design Primers \| Restriction Fragment Map \| Restriction Fragment Sizes \| Six-Frame Translation
S288C vs. other species	Fungal Alignment \| BLASTN vs. fungi \| BLASTP at NCBI \| BLASTP vs. fungi \| Synteny Viewer
S288C vs. other strains	Strain Alignment

Resources

External Links	All Associated Seq \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| Search all NCBI (Entrez) \| UniProtKB

Primary SGDID	S000004249

References cited on this page View Complete Literature Guide for HSP60

1)	Reading DS, et al. (1989) Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337(6208):655-9
2)	Rospert S, et al. (1993) Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria. Proc Natl Acad Sci U S A 90(23):10967-71
3)	Cheng MY, et al. (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208):620-5
4)	Mueller DM, et al. (1987) Temperature sensitive pet mutants in yeast Saccharomyces cerevisiae that lose mitochondrial RNA. Curr Genet 11(5):359-67
5)	Sanyal A, et al. (1995) Heat shock protein HSP60 can alleviate the phenotype of mitochondrial RNA-deficient temperature-sensitive mna2 pet mutants. Mol Gen Genet 246(1):56-64
6)	Cheng MY, et al. (1990) The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348(6300):455-8
7)	Koll H, et al. (1992) Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68(6):1163-75
8)	Kaufman BA, et al. (2003) A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae. J Cell Biol 163(3):457-61
9)	Reinders J, et al. (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
10)	Johnson RB, et al. (1989) Cloning and characterization of the yeast chaperonin HSP60 gene. Gene 84(2):295-302