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bacteria:t3e:xopai [2023/12/08 14:06] – [References] rkoebnik | bacteria:t3e:xopai [2025/02/12 23:26] (current) – jfpothier | ||
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- | ====== XopAI ====== | + | ====== |
- | Author: [[https:// | + | Author: [[https:// |
- | Internal reviewer: \\ | + | |
- | Expert reviewer: **WANTED!** | + | |
Class: XopAI\\ | Class: XopAI\\ | ||
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=== How discovered? === | === How discovered? === | ||
- | Based on the complete genome sequence, XopAI (XAC3230) was proposed as a Hrp regulon candidate (da Silva //et al.//, 2002). Based on homology to effectors from Pseudomonas syringae and a strongly conserved 43‐amino‐acid N‐terminal domain that is also found in the N‐termini of effectors in class XopE and XopJ, it was proposed to be a T3E (White //et al.//, 2009). | + | Based on the complete genome sequence, XopAI (XAC3230) was proposed as a Hrp regulon candidate (da Silva //et al.//, 2002). |
+ | |||
+ | Co-regulation of //xopAI// with other HrpG-controlled genes was also proposed by Noël //et al.// (2006) based on the observation that 200 bp of the 5' sequence including promoter and coding regions of //xopE2// (// | ||
+ | |||
+ | Based on homology to effectors from //Pseudomonas syringae// and a strongly conserved 43‐amino‐acid N‐terminal domain that is also found in the N‐termini of effectors in class XopE and XopJ, XopAI was proposed to be a T3E (Stavrinides //et al.//, 2006; White //et al.//, 2009). | ||
=== (Experimental) evidence for being a T3E === | === (Experimental) evidence for being a T3E === | ||
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=== Regulation === | === Regulation === | ||
- | Unknown. | + | Using microarrays, |
=== Phenotypes === | === Phenotypes === | ||
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XopAI was predicted to be a member of the arginine-specific mono-ADP-ribosyltransferase (mART) family. However, the crystal structure of XopAI revealed an altered active site that is unsuitable to bind the cofactor NAD+, but with the capability to capture an arginine-containing peptide from XopAI itself. Based on this finding, it was proposed that XopAI may not be a qualified mART, and it would exert different effects on host cells (Liu //et al.//, 2019). | XopAI was predicted to be a member of the arginine-specific mono-ADP-ribosyltransferase (mART) family. However, the crystal structure of XopAI revealed an altered active site that is unsuitable to bind the cofactor NAD+, but with the capability to capture an arginine-containing peptide from XopAI itself. Based on this finding, it was proposed that XopAI may not be a qualified mART, and it would exert different effects on host cells (Liu //et al.//, 2019). | ||
- | Structural homologs of XopAI are, among others, the HopU1 (// | + | Structural homologs of XopAI are, among others, the HopU1 (// |
=== Interaction partners === | === Interaction partners === | ||
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=== In xanthomonads === | === In xanthomonads === | ||
- | XopAI is conserved in the Citrus canker strains, including //X. citri// pv. //citri// and //X. citri// pv. // | + | XopAI is conserved in the Citrus canker strains, including //X. citri// pv. //citri// and //X. citri// pv. // |
- | XopAI homologs were also found in //X. citri// pv. //bilvae// and //X. citri// pv. // | + | XopAI homologs were also found in //X. citri// pv. //bilvae// and //X. citri// pv. // |
=== In other plant pathogens/ | === In other plant pathogens/ | ||
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da Silva AC, Ferro JA, Reinach FC, Farah CS, Furlan LR, Quaggio RB, Monteiro-Vitorello CB, Van Sluys MA, Almeida NF, Alves LM, do Amaral AM, Bertolini MC, Camargo LE, Camarotte G, Cannavan F, Cardozo J, Chambergo F, Ciapina LP, Cicarelli RM, Coutinho LL, Cursino-Santos JR, El-Dorry H, Faria JB, Ferreira AJ, Ferreira RC, Ferro MI, Formighieri EF, Franco MC, Greggio CC, Gruber A, Katsuyama AM, Kishi LT, Leite RP, Lemos EG, Lemos MV, Locali EC, Machado MA, Madeira AM, Martinez-Rossi NM, Martins EC, Meidanis J, Menck CF, Miyaki CY, Moon DH, Moreira LM, Novo MT, Okura VK, Oliveira MC, Oliveira VR, Pereira HA, Rossi A, Sena JA, Silva C, de Souza RF, Spinola LA, Takita MA, Tamura RE, Teixeira EC, Tezza RI, Trindade dos Santos M, Truffi D, Tsai SM, White FF, Setubal JC, Kitajima JP (2002). Comparison of the genomes of two // | da Silva AC, Ferro JA, Reinach FC, Farah CS, Furlan LR, Quaggio RB, Monteiro-Vitorello CB, Van Sluys MA, Almeida NF, Alves LM, do Amaral AM, Bertolini MC, Camargo LE, Camarotte G, Cannavan F, Cardozo J, Chambergo F, Ciapina LP, Cicarelli RM, Coutinho LL, Cursino-Santos JR, El-Dorry H, Faria JB, Ferreira AJ, Ferreira RC, Ferro MI, Formighieri EF, Franco MC, Greggio CC, Gruber A, Katsuyama AM, Kishi LT, Leite RP, Lemos EG, Lemos MV, Locali EC, Machado MA, Madeira AM, Martinez-Rossi NM, Martins EC, Meidanis J, Menck CF, Miyaki CY, Moon DH, Moreira LM, Novo MT, Okura VK, Oliveira MC, Oliveira VR, Pereira HA, Rossi A, Sena JA, Silva C, de Souza RF, Spinola LA, Takita MA, Tamura RE, Teixeira EC, Tezza RI, Trindade dos Santos M, Truffi D, Tsai SM, White FF, Setubal JC, Kitajima JP (2002). Comparison of the genomes of two // | ||
+ | |||
+ | de Laia ML, Moreira LM, Gonçalves JF, Ferro MI, Pinto Rodrigues AC, dos Santos JN, Felestrino ÉB, Ferro JA (2019). Gene expression analysis identifies hypothetical genes that may be critical during the infection process of // | ||
+ | Electron. J. Biotechnol. 42: 30-41. DOI: 10.1016/ | ||
Fu Z (2008). // | Fu Z (2008). // |