|Gene:||yajL||Accession Numbers: G198 (EcoCyc), b0424, ECK0418|
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].
|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
|Biological Process:||GO:0009408 - response to heat
GO:0034599 - cellular response to oxidative stress [Kthiri10]
GO:0042026 - protein refolding [Kthiri10]
GO:0042254 - ribosome biogenesis [UniProtGOA11a, Kthiri10a]
GO:0006950 - response to stress [UniProtGOA11a]
|Molecular Function:||GO:0042803 - protein homodimerization activity [Le12]|
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09, Ishihama08, LopezCampistrou05]|
|MultiFun Terms:||cell processes → adaptations → other (mechanical, nutritional, oxidative stress)|
|information transfer → protein related → chaperoning, repair (refolding)|
|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]|
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
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
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
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
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