ECM10/YEL030W Summary Help

Standard Name ECM10 1
Systematic Name YEL030W
Alias SSC3
Feature Type ORF, Verified
Description Heat shock protein of the Hsp70 family; localized in mitochondrial nucleoids, plays a role in protein translocation, interacts with Mge1p in an ATP-dependent manner; overexpression induces extensive mitochondrial DNA aggregations; ECM10 has a paralog, SSC1, that arose from the whole genome duplication (2, 3, 4 and see Summary Paragraph)
Name Description ExtraCellular Mutant 1
Chromosomal Location
ChrV:94644 to 96578 | ORF Map | GBrowse
Gene Ontology Annotations All ECM10 GO evidence and references
  View Computational GO annotations for ECM10
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
44 total interaction(s) for 40 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 28
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2

Genetic Interactions
  • Negative Genetic: 11
  • Phenotypic Suppression: 1
  • Synthetic Growth Defect: 1

Expression Summary
Length (a.a.) 644
Molecular Weight (Da) 70,084
Isoelectric Point (pI) 6.14
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrV:94644 to 96578 | ORF Map | GBrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1935 94644..96578 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 | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000756

SSC1, SSQ1, and ECM10 encode chaperone proteins of the HSP70 family that localize to the mitochondria (2 and reviewed in 5). In addition to these three mitochondrial HSP70s, S. cerevisiae cells also synthesize nine cytosolic HSPs (encoded by SSA1, SSA2, SSA3, SSA4, SSB1, SSB2, SSE1, SSE2, SSZ1) and two that are found in the ER (KAR2, LHS1). HSP70 is a large family of proteins that has been evolutionarily conserved from bacteria (DnaK) to humans (HSP72/73). HSP70 proteins were originally classified based upon their induction by heat shock and their size of ~70kDa. The main function of these proteins is to serve as molecular chaperones, binding unfolded peptides to assist in proper folding and prevent aggregation/misfolding (reviewed in 6 and 7). HSP70s are also involved in disassembling aggregates of misfolded proteins, translocating select proteins into the mitochondria and ER, and degrading aberrant proteins (reviewed in 8, 7, and 6).

ECM10 was originally identified in a screen for genes involved in cell wall biogenesis (1). Ecm10p localizes to mitochondrial nucleoids and is suggested to function in mitochondrial protein import (3, 2). Ecm10p displays a high degree of similarity to the other mitochondrial HSP70 proteins (82% and 54% amino acid identity with Ssc1p and Ssq1p, respectively) and like all HSP70s, has an N-terminal ATPase domain and a C-terminal peptide-binding domain (2). Like Ssc1p and Ssq1p, Ecm10p interacts with the nucleotide exchange factor Mge1p in an ATP-dependent manner (2, 9). Overexpression of Ecm10p results in extensive mitochondrial DNA aggregations. While ecm10 deletion mutants are viable, ecm10 ssc1 double null mutants exhibit synthetic growth defects (3, 2).

Last updated: 2006-02-09 Contact SGD

References cited on this page View Complete Literature Guide for ECM10
1) Lussier M, et al.  (1997) Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae. Genetics 147(2):435-50
2) Baumann F, et al.  (2000) Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae. FEBS Lett 487(2):307-12
3) Sakasegawa Y, et al.  (2003) Ecm10p localizes in yeast mitochondrial nucleoids and its overexpression induces extensive mitochondrial DNA aggregations. Biochem Biophys Res Commun 309(1):217-21
4) 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
5) Voos W and Rottgers K  (2002) Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592(1):51-62
6) Bukau B and Horwich AL  (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92(3):351-66
7) Becker J and Craig EA  (1994) Heat-shock proteins as molecular chaperones. Eur J Biochem 219(1-2):11-23
8) Hartl FU  (1996) Molecular chaperones in cellular protein folding. Nature 381(6583):571-9
9) Lutz T, et al.  (2001) The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J Mol Biol 307(3):815-25