YJL068C Summary

Systematic Name	YJL068C
Feature Type	ORF, Verified
Description	Non-essential intracellular esterase that can function as an S-formylglutathione hydrolase; may be involved in the detoxification of formaldehyde, which can be metabolized to S-formylglutathione; similar to human esterase D (1, 2 and see Summary Paragraph) Also known as: SFGH 3

Chromosomal Location	ChrX:313915 to 313016 \| ORF Map \| GBrowse
	Note: this feature is encoded on the Crick strand.

Gene Ontology Annotations All YJL068C GO evidence and references

	View Computational GO annotations for YJL068C
Molecular Function
Manually curated	S-formylglutathione hydrolase activity (IDA)
Biological Process
Manually curated	formaldehyde catabolic process (IMP)
Cellular Component
Manually curated	cytosol (IDA)

Pathways	formaldehyde oxidation II (glutathione-dependent)

Mutant phenotypes All YJL068C Phenotype evidence and references

Classical genetics
null	viable
Large-scale survey
null	anaerobic growth: decreased competitive fitness: increased endocytosis: decreased haploinsufficient Fus-Mid-GFP distribution: abnormal viable
Resources	PROPHECY \| SCMD \| ScreenTroll \| Yeast Fitness Database

interactions All YJL068C Interaction evidence and references

	83 total interaction(s) for 61 unique genes/features.
Physical Interactions	Affinity Capture-MS: 3 Co-crystal Structure: 1 PCA: 2 Reconstituted Complex: 1 Two-hybrid: 1
Genetic Interactions	Negative Genetic: 73 Positive Genetic: 2
Resources	BioGRID \| BOND \| BioPIXIE \| CYC2008 (complexes) \| Complexome \| DIP \| DRYGIN \| GeneMANIA \| InterologFinder

Expression Summary


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

Protein Information All YJL068C 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

ChrX:313915 to 313016 | |

Note: this feature is encoded on the Crick strand.

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..900	313915..313016	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 \| E.C. \| Entrez Gene \| Entrez RefSeq Protein \| MIPS \| Search all NCBI (Entrez) \| UniProtKB

Primary SGDID	S000003604

SUMMARY PARAGRAPH for YJL068C

Yjl068cp is an esterase with S-formylglutathione hydrolase activity which appears to be involved in formaldehyde detoxification (2). Purified Yjl068cp is able to hydroyze a variety of substrates, including S-formylglutathione, carboxyfluorescein diacetate, 4-methylumbelliferyl acetate, p-nitrophenyl acetate, and alpha-naphthyl acetate, but is unable to hydrolyze alpha-naphthyl laurate and alpha-naphthyl oleate (2). YJL068C is induced in response to methyl methanesulfonate (MMS) (4) and neocarzinostatin (NCS), which possesses a regulatory function on the metabolism of DNA and exhibits potent antiproliferative activity in mammalian cells and against gram-positive organisms (5). Null mutants in YJL068C are viable, but display reduced esterase activity and slow growth in the presence of formaldehyde (1, 2). Yjl068cp exhibits similarity to the S-formylglutathione hydrolases of Paracoccus denitrificans, Haemophilus influenzae, Escherichia coli and humans (6, 1).

About glutathione-dependent formaldehyde oxidation

Formaldehyde is formed by oxidative demethylation reactions in many plants and methylotrophic organisms, but Saccharomyces cerevisiae is a nonmethylotrophic yeast and cannot metabolize methanol to formaldehyde. However, S. cerevisiae is exposed to exogenous formaldehyde from plant material or in polluted air and water.

Concentrations of formaldehyde of 1mM or higher are cytostatic or cytotoxic to haploid wild-type cells. Any free formaldehyde in vivo spontaneously reacts with glutathione to form S-hydroxymethylglutathione (7, 8, 2). The level of enzymes involved in the degradation of formaldehyde, such as Sfa1p and Yjl068p, determine the level of formaldehyde toxicity, and cells overproducing Sfa1p are resistant to formaldehyde and null mutants in either sfa1 or yjl068c are hypersensitive to formaldehyde. Sfa1p is induced in response to chemicals such as formaldehyde (FA), ethanol and methyl methanesulphonate, and Yjl068p is also induced in response to chemical stresses (9, 8, 2, 10, 11, 4, 5).

Formate dehydrogenase is encoded by FDH1/YOR388C and FDH2. In some strain backgrounds of S. cerevisiae, FDH2 is encoded by a continuous open reading frame comprised of YPL275W and YPL276W. However, in the systematic sequence of S288C, FDH2 is represented by these two separate open reading frames due to an in frame stop codon (12).

Last updated: 2006-01-24

References cited on this page View Complete Literature Guide for

1)	Vandenbol M and Portetelle D (1999) Disruption of six ORFs on Saccharomyces cerevisiae chromosome X: the YJL069c gene of unknown function is essential to cell viability. Yeast 15(13):1411-7
2)	Degrassi G, et al. (1999) Purification and properties of an esterase from the yeast Saccharomyces cerevisiae and identification of the encoding gene. Appl Environ Microbiol 65(8):3470-2
3)	Legler PM, et al. (2012) A role for His-160 in peroxide inhibition of S. cerevisiae S-formylglutathione hydrolase: evidence for an oxidation sensitive motif. Arch Biochem Biophys 528(1):7-20
4)	Jelinsky SA and Samson LD (1999) Global response of Saccharomyces cerevisiae to an alkylating agent. Proc Natl Acad Sci U S A 96(4):1486-91
5)	Schaus SE, et al. (2001) Gene transcription analysis of Saccharomyces cerevisiae exposed to neocarzinostatin protein-chromophore complex reveals evidence of DNA damage, a potential mechanism of resistance, and consequences of prolonged exposure. Proc Natl Acad Sci U S A 98(20):11075-80
6)	Harms N, et al. (1996) S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification? J Bacteriol 178(21):6296-9
7)	Achkor H, et al. (2003) Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis. Plant Physiol 132(4):2248-55
8)	Grey M, et al. (1996) Overexpression of ADH1 confers hyper-resistance to formaldehyde in Saccharomyces cerevisiae. Curr Genet 29(5):437-40
9)	Wehner E and Brendel M (1993) Formaldehyde lacks genotoxicity in formaldehyde-hyperresistant strains of the yeast Saccharomyces cerevisiae. Mutat Res 289(1):91-6
10)	Wehner EP, et al. (1993) Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product. Mol Gen Genet 237(3):351-8
11)	Gompel-Klein P, et al. (1989) Molecular characterization of the two genes SNQ and SFA that confer hyperresistance to 4-nitroquinoline-N-oxide and formaldehyde in Saccharomyces cerevisiae. Curr Genet 16(2):65-74
12)	Overkamp KM, et al. (2002) Functional analysis of structural genes for NAD(+)-dependent formate dehydrogenase in Saccharomyces cerevisiae. Yeast 19(6):509-20