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Escherichia coli K-12 substr. MG1655 Protein: chaperone, protecting proteins in response to oxidative stress

Gene: yajL Accession Numbers: G198 (EcoCyc), b0424, ECK0418

Synonyms: thiJ

Regulation Summary Diagram: ?

Subunit composition of chaperone, protecting proteins in response to oxidative stress = [YajL]2
         chaperone, protecting proteins in response to oxidative stress = YajL

The YajL protein functions as a covalent chaperone for sulfenylated proteins [Kthiri10, Le12, Gautier12]. YajL forms mixed disulfides with cellular proteins in response to oxidative stress; its cellular targets include a number or ribosomal proteins as well as members of the cellular thiol proteome, including aconitase and Fe-S cluster-containing subunits of dehydrogenases [Le12, Gautier12]. Free YajL can be regenerated by reduced glutathione or dihydrolipoamide, but not thioredoxin [Gautier12].

YajL was mistakenly identified as ThiJ and was implicated in thiamine biosynthesis. However, later experiments showed that the original complementation phenotype was due to the neighboring gene, thiI [Mueller98].

A crystal structure of YajL has been solved at 1.1 Å resolution. YajL shows similarity in the overall structure [Wilson05a] and in predicted functional sites [Wei07] to the human oncogene and neuroprotective protein DJ-1. YajL is a dimer in solution; the C47 residue is required for dimerization [Le12].

A yajL mutant is more sensitive to oxidative stress than wild type and accumulates aggregated proteins under aerobic conditions [Kthiri10]. The conserved C106 residue is important for the formation of mixed disulfides [Kthiri10, Gautier12]. A yajL mutant shows altered ribosome profiles and increased frameshifting after oxidative stress [Kthiri10a] and contains higher levels of sulfenylated proteins than wild type [Gautier12]. Transcriptional profiling of a yajL mutant shows that loss of yajL triggers a global stress response [Messaoudi13].

yajL shows differential codon adaptation, resulting in differential translation efficiency signatures, in thermophilic microbes. It was therefore predicted to play a role in the heat shock response. A yajL deletion mutant was shown to be more sensitive than wild-type specifically to heat shock, but not other stresses [Krisko14].

Locations: cytosol

Map Position: [442,275 <- 442,865] (9.53 centisomes)
Length: 591 bp / 196 aa

Molecular Weight of Polypeptide: 20.777 kD (from nucleotide sequence)

Molecular Weight of Multimer: 52.0 kD (experimental) [Le12]

Unification Links: ASAP:ABE-0001472 , EchoBASE:EB3057 , EcoGene:EG13272 , EcoliWiki:b0424 , ModBase:Q46948 , OU-Microarray:b0424 , PortEco:yajL , PR:PRO_000024059 , Pride:Q46948 , Protein Model Portal:Q46948 , RefSeq:NP_414958 , RegulonDB:G198 , SMR:Q46948 , String:511145.b0424 , UniProt:Q46948

Relationship Links: InterPro:IN-FAMILY:IPR002818 , InterPro:IN-FAMILY:IPR006287 , PDB:Structure:2AB0 , Pfam:IN-FAMILY:PF01965

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009408 - response to heat Inferred from experiment [Krisko14]
GO:0034599 - cellular response to oxidative stress Inferred from experiment [Kthiri10]
GO:0042026 - protein refolding Inferred from experiment [Kthiri10]
GO:0042254 - ribosome biogenesis Inferred from experiment Inferred by computational analysis [UniProtGOA11, Kthiri10a]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0042803 - protein homodimerization activity Inferred from experiment [Le12]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

MultiFun Terms: cell processes adaptations other (mechanical, nutritional, oxidative stress)
information transfer protein related chaperoning, repair (refolding)

Essentiality data for yajL knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Created 20-Dec-2011 by Keseler I , SRI International
Last-Curated ? 16-Jan-2013 by Keseler I , SRI International

Sequence Features

Feature Class Location Citations Comment
Cysteine-sulfinic-acid-Modification 106
UniProt: Cysteine sulfinic acid (-SO2H).
Mutagenesis-Variant 106
[Kthiri10, UniProt11]
Alternate sequence: C → D; UniProt: Does not complement a disruption mutant.
Alternate sequence: C → A; UniProt: Does not complement a disruption mutant.

Gene Local Context (not to scale): ?

Transcription Unit:


Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Suzanne Paley on Mon Apr 14, 2003:
Comment from EcoGene: Function unknown, PfpI/HchA protease/chaperone family; not involved in thiamine metabolism. YajL has been mistakenly described as ThiJ, involved in thiamine metabolism. This phenotype is now attributed to the adjacent thiI gene. This error is acknowledged by T. Begley in a personal communication cited in the discussion section of Mueller et al., NAR 26:2606-10 (1998).
10/20/97 Gene b0424 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene G198.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gautier12: Gautier V, Le HT, Malki A, Messaoudi N, Caldas T, Kthiri F, Landoulsi A, Richarme G (2012). "YajL, the prokaryotic homolog of the Parkinsonism-associated protein DJ-1, protects cells against protein sulfenylation." J Mol Biol 421(4-5);662-70. PMID: 22321799

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Krisko14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

Kthiri10: Kthiri F, Le HT, Gautier V, Caldas T, Malki A, Landoulsi A, Bohn C, Bouloc P, Richarme G (2010). "Protein aggregation in a mutant deficient in YajL,the bacterial homolog of the parkinsonism-associated protein DJ-1." J Biol Chem 285(14):10328-36. PMID: 20124404

Kthiri10a: Kthiri F, Gautier V, Le HT, Prere MF, Fayet O, Malki A, Landoulsi A, Richarme G (2010). "Translational defects in a mutant deficient in YajL, the bacterial homolog of the parkinsonism-associated protein DJ-1." J Bacteriol 192(23);6302-6. PMID: 20889753

Le12: Le HT, Gautier V, Kthiri F, Malki A, Messaoudi N, Mihoub M, Landoulsi A, An YJ, Cha SS, Richarme G (2012). "YajL, prokaryotic homolog of parkinsonism-associated protein DJ-1, functions as a covalent chaperone for thiol proteome." J Biol Chem 287(8);5861-70. PMID: 22157000

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Messaoudi13: Messaoudi N, Gautier V, Kthiri F, Lelandais G, Mihoub M, Joseleau-Petit D, Caldas T, Bohn C, Tolosa L, Rao G, Tao K, Landoulsi A, Bouloc P, Richarme G (2013). "Global stress response in a prokaryotic model of DJ-1-associated Parkinsonism." J Bacteriol 195(6);1167-78. PMID: 23292772

Mueller98: Mueller EG, Buck CJ, Palenchar PM, Barnhart LE, Paulson JL (1998). "Identification of a gene involved in the generation of 4-thiouridine in tRNA." Nucleic Acids Res 26(11);2606-10. PMID: 9592144

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wei07: Wei Y, Ringe D, Wilson MA, Ondrechen MJ (2007). "Identification of functional subclasses in the DJ-1 superfamily proteins." PLoS Comput Biol 3(1);e10. PMID: 17257049

Wilson05a: Wilson MA, Ringe D, Petsko GA (2005). "The Atomic Resolution Crystal Structure of the YajL (ThiJ) Protein from Escherichia coli: A Close Prokaryotic Homologue of the Parkinsonism-associated Protein DJ-1." J Mol Biol 353(3);678-91. PMID: 16181642

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Jan 24, 2015, biocyc12.