ZIM17 Zim17p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: ZIM17
Official Full Name: Zim17p
Primary source: SGD:S000005254
Locus tag: YNL310C
See related: AllianceGenome:SGD:S000005254; FungiDB:YNL310C; VEuPathDB:YNL310C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: HEP1; TIM15
Summary: Enables protein-folding chaperone binding activity. Involved in several processes, including protein folding; protein import into mitochondrial matrix; and protein stabilization. Located in mitochondrial matrix. Orthologous to human DNLZ (DNL-type zinc finger). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See ZIM17 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (51907..52431, complement)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

the induction of the zim17 mutant phenotype leads to strong import defects for Ssc1-dependent matrix-targeted precursor proteins that correlate with a significantly reduced binding of newly imported substrate proteins to Ssc1.
Title: The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.
Zn(2+) induced TIM15 folding is essential for its function and likely occurs in mitochondrial matrix where high concentrations of Zn(2+) were reported.
Title: Zinc induced folding is essential for TIM15 activity as an mtHsp70 chaperone.
Arabidopsis Zinc Ribbon 3 is the ortholog of yeast mitochondrial HSP70 escort protein HEP1 and belongs to an ancient protein family in mitochondria and plastids.
Title: Arabidopsis Zinc Ribbon 3 is the ortholog of yeast mitochondrial HSP70 escort protein HEP1 and belongs to an ancient protein family in mitochondria and plastids.
Human DNLZ partially complements the growth of Deltazim17 Saccharomyces cerevisiae.
Title: The DNLZ/HEP zinc-binding subdomain is critical for regulation of the mitochondrial chaperone HSPA9.
Cells lacking Zim17 (Tim15/Hep1), have limited respiration activity, mimic the metabolic response to iron starvation and suffer a dramatic increase in nuclear genome recombination.
Title: Zim17/Tim15 links mitochondrial iron-sulfur cluster biosynthesis to nuclear genome stability.
example of a "fractured" J-protein, where a protein like Zim17 contributes a zinc finger domain to Type III J-proteins
Title: Zim17, a novel zinc finger protein essential for protein import into mitochondria.
findings suggest that Zim17 plays a specific role in preventing protein aggregation in the mitochondrial matrix, and that aggregation of Hsp70s causes pleiotropic effects on protein biogenesis and mitochondrial morphology
Title: Inactivation of the mitochondrial heat shock protein zim17 leads to aggregation of matrix hsp70s followed by pleiotropic effects on morphology and protein biogenesis.
Tim15/Zim17 cooperates with mtHsp70 to facilitate import of presequence-containing proteins into the matrix.
Title: Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in mitochondrion organization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein import into mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial matrix	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein stabilization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in response to unfolded protein	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in mitochondrial inner membrane	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Zim17p

NP_014089.2

Protein co-chaperone with a zinc finger motif; essential for protein import into mitochondria; may act with Pam18p to facilitate recognition and folding of imported proteins by Ssc1p (mtHSP70) in the mitochondrial matrix; required for the maintenance of Ssc1p solubility and assists in the functional interaction of Ssc1p with substrate proteins