You're using an outdated browser. Please upgrade to a modern browser for the best experience.
Submitted Successfully!
Thank you for your contribution! You can also upload a video entry or images related to this topic. For video creation, please contact our Academic Video Service.
Version Summary Created by Modification Content Size Created at Operation
1
jiandong bao
 -- 1341 2022-05-06 09:52:44 |
2 layout
Camila Xu
 Meta information modification 1341 2022-05-06 10:00:03 | |
3 no correction
Lin Li
 Meta information modification 1341 2022-05-07 07:21:05 | |
4 layout
Camila Xu
 + 22 word(s) 1363 2022-05-13 05:01:08 |

Video Upload Options

We provide professional Academic Video Service to translate complex research into visually appealing presentations. Would you like to try it?
No, upload directly Yes

Confirm

Are you sure to Delete?
Yes No
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
Bao, J.; Lin, F.; Li, L.; , .; Wang, J. Recognition and Regulation of Pathogenic Fungi. Encyclopedia. Available online: https://encyclopedia.pub/entry/22649 (accessed on 13 June 2025).
Bao J, Lin F, Li L,  , Wang J. Recognition and Regulation of Pathogenic Fungi. Encyclopedia. Available at: https://encyclopedia.pub/entry/22649. Accessed June 13, 2025.
Bao, Jiandong, Fucheng Lin, Lin Li,  , Jiaoyu Wang. "Recognition and Regulation of Pathogenic Fungi" Encyclopedia, https://encyclopedia.pub/entry/22649 (accessed June 13, 2025).
Bao, J., Lin, F., Li, L., , ., & Wang, J. (2022, May 06). Recognition and Regulation of Pathogenic Fungi. In Encyclopedia. https://encyclopedia.pub/entry/22649
Bao, Jiandong, et al. "Recognition and Regulation of Pathogenic Fungi." Encyclopedia. Web. 06 May, 2022.
Recognition and Regulation of Pathogenic Fungi
Edit
This entry is adapted from the peer-reviewed paper 10.3390/ijms23094658

The interaction between pathogenic fungi and plants is a complex process. From the perspective of pathogenic fungi, pathogenic fungi are involved in the regulation of pathogenicity by surface signal recognition proteins, MAPK signaling pathways, transcription factors, and pathogenic factors in the process of infecting plants.

pathogenic fungi plants interaction penetration

1. Introduction

Pathogenic fungi invade plants in four main steps: adhesion on host surface, form infection structure, invasion of host, colonization and expansion within host. Some pathogenic fungi can even produce metabolites that are toxic to their hosts, and these substances are considered to be one of the main causes of plant diseases. Different pathogenic genes cause different infection processes and metabolic regulation modes. The interactions between plants and pathogenic fungi can be divided into incompatibility and affinity. In non-compatible interactions, local necrotic spots with obvious differences from surrounding healthy tissues are formed at the infection site, namely hyper-sensitive reaction (HR) [1]. In affinity interaction, some fungi take advantage of stomata or trauma on the host surface to invade, usually producing infection structures formed by specialized hyphae. Infection cushion, appressorium, and haustorium help pathogenic fungi invade and establish parasitic relationships with hosts, resulting in plant infection [2].
The innate immune system of plants consists of two main immune responses [3]. One is nonspecific defense response: pattern recognition receptors (PRRs) of plants can recognize highly conserved macromolecular substances common to pathogenic microorganisms which are called pathogen-associated molecular patterns (PAMPs), such as flagella and polysaccharides [4][5]. When PAMPs are recognized by PRRs, relative signal transduction pathways are activated and then induce defense response to limit the invasion of pathogenic microorganisms. This process is called PAMP-triggered immunity (PTI) response [6]. The second is specific defense response: In order to successfully infect plants, pathogenic microorganisms have evolved effector proteins to inhibit the immune response induced by PAMPs. At the same time, plants have evolved R genes to monitor and identify effectors, cause hypersensitive response (HR) and limit the invasion of pathogens. This resistance is called effector-triggered immunity (ETI) [3].

2. Signal Recognition of Pathogenic Fungi Infection Process

Signaling pathway refers to a series of enzymatic reaction pathways that can transmit extracellular signals into the cell through the cell membrane. Receptors on the cell membrane sense external signals. In organisms, these receptor proteins include ion channel receptors, G-protein-coupled receptors (GPCR), tyrosine kinase receptors, and receptors that regulate gene expression. In fungi, heterotrimer G protein participates in the regulation of vegetative growth, pathogenicity, sporulation, and differentiation of infection structure by regulating the activities of adenylate cyclase and phospholipase and ion channels [7][8][9]. In Ustilago maydis, heterotrimer G proteins and GPCR are involved in mating and pathogenicity by regulating hormone response and cAMP-dependent signaling pathways [10][11]. In Aspergillus fumigatus, the Gα subunit GpaB positively regulates conidia survival and PksP expression in macrophages [12]. Phenotypes of the gpaB mutant and the adenylate cyclase mutant acyA suggest that a gpaB mediated cAMP-dependent signaling pathway is involved in the pathogenesis of A. fumigatus [12][13]. In Cryphonectria parasitica, Gα protein Cpg-1 is essential for pathogenesis. Cpg-1 is involved in the growth and sporulation of trophic mycelia, and the pathogenic process is regulated by a pathway independent of Gβγ [14][15][16]. In contrast, Gβ subunit Cpgb-1 positively regulates pathogenicity but does not affect vegetative growth [17]. In Cryptococcus neoformans, adenylate cyclase Cac1 positively regulates the formation and toxicity of the capsule [18][19]. On the other hand, Gβ subunit Gpb1 is not required for pod formation, pigment synthesis, or toxicity [20]. Although defective capsular formation is observed in the gpr4 GPCR mutant, pigment and toxicity remained unchanged [19].
The MAPK cascade pathway is located in the center of the cell signal transmission network, and is involved in regulating cell growth and differentiation, photosynthesis, metabolism, synthesis and release of neurotransmitters, adaptation to adverse environment, infection of pathogens, and other physiological processes [21][22][23][24][25]. In many pathogenic fungi, the HOG pathway mainly plays a role in adapting to high osmotic pressure in the external environment. In Neurospora crassa, it is found that the HOG pathway mainly consists of osmotically responsive histidine kinase Os1, histidine phosphate group transfer proteins Hpt1, RRG1/2, and downstream phosphoric acid coupling systems of Os4, Os5, and Os2 [26][27][28]. Studies have found that the HOG pathway in N. crassa is not only related to environmental stress, but also regulates the production of bacterial pigments, resistance to diimide fungicides, and pathogenicity of bacteria. The HOG pathway of Botrytis cinerea is also reported to be sensitive to osmotic stress, DCFs, and pathogenicity of the pathogen to different hosts [29][30]. However, Osm1 (homologous protein of Hog1), a key element of the HOG pathway in Magnaporthe oryzae, is associated with drug sensitivity and osmotic stress, but is not closely associated with pathogen pathogenicity [31][32]. Fus3/Kss1 pathway not only has an important relationship with the sexual reproduction of pathogenic fungi but also plays an important role in regulating the pathogenicity of pathogenic fungi. In Aspergillus nidulans, although the scaffold protein Ste5 is missing, it can still form the complex AnSte50-AnSte11-AnSte7-AnFus3. After the complex is activated by upstream signals, AnFus3 will enter the nucleus and activate the activity of AnSteA (homologous protein of Ste12) and AnVeA. Activated AnSteA can regulate mycelial fusion and sexual reproduction of A. nidulans, while activated AnVeA can regulate secondary metabolism of A. nidulans [33][34][35]. In M. oryzae, mutants of pmk1 (homologous protein of Fus3) cannot produce appressorium and cannot penetrate the host surface [36][37]. The CWI pathway is a kind of MAPK signaling pathway that has been studied well in pathogenic fungi. Kinase Slt2, a core component of the CWI pathway, has been found to regulate cell wall integrity in Alternaria brassicicola, A. nidulans, and M. oryzae [38][39][40][41]. Slt2 has also been found to be significantly associated with the pathogenicity of many pathogens, such as Candida albicans [42].

3. Regulation of Pathogenic Processes by Transcription Factors of Pathogenic Fungi

Transcription factors are the largest family of trans-acting factors. In a broad sense, all transcription-related proteins except RNA polymerase itself can be classified as transcription factors [43]. The zinc finger protein family is the most widely distributed in the eukaryotic transcription factors family and can generally be divided into zinc finger and zinc cluster structure. Zn2Cys6 transcription factor is a kind of zinc finger protein peculiar to fungi. Colletotrichum melanin regulation (CMR) and Pigment of M. oryzae (PIG) encodes a protein that contains both zinc fingers and zinc clusters, both of which are involved in melanin synthesis [44]. The AlcR protein of A. nidulans contains Zn2Cys6 zinc clusters, and its main function is mainly related to ethanol metabolism [45].
bZIP transcription factors in A. nidulans are involved in the regulation of secondary metabolism, sexual reproduction, and stress response [46]. The bZIP protein in N. crassa is associated with sulfur utilization and oxidative pressure reaction [47][48]. The bZIP transcription factor in A. fumigatus mainly regulates asexual reproduction, gelatoxin production, sulfur assimilation, and infection [49][50]. FgAp1, a bZIP transcription factor in Fusarium graminearum, is associated with oxidative pressure response and toxin synthesis. FoMeab, a bZIP protein from Fusarium oxysporum, is involved in regulating nitrogen cycling pathways [51]. In M. oryzae, bZIP transcription factor genes coordinate the physiological processes such as growth and development, conidiation, appressorium formation, infection, and pathogenicity [52].
Homologous heteromorphic box structure transcription factors proteins generally have two protein binding regions, and conformational changes after binding to regulatory proteins; thus, regulating DNA binding activity [53]. In U. maydis, homologous genes are mainly involved in the regulation of linear growth, sexual reproduction, and infection of host plants [54]. In Podospora anseria, the homologous heteromorphic box gene PAH1 regulates mycelia extension growth and male spore production, and its gene deletion mutants grow slowly and the mycelia is compact [55]. In M. oryzae, eight homologous heteromorphic box genes are identified and named as MoHox1-MoHox8, in which ΔMohox1, ΔMohox4, and ΔMohox6 grew at a slower rate, and aerial hyphae were scarce. ΔMohox8 appressorium penetration decreased and pathogenicity decreased. ΔMohox7 does not produce functional appressorium in either germ tube or mycelium tip, resulting in a complete loss of pathogenicity [56]. bHLH transcription factors are highly conserved transcription factors in eukaryotes. In N. crassa, bHLH transcription factor CHC-1 is associated with CO2-mediated negative regulation of sporulation [57]. In A. nidulans, AnBH1 regulates penicillin synthesis, and DevR regulates sexual and asexual reproduction [58][59]. SclR in Aspergillus oryzae promotes sclerotia. EcdR is related to the early differentiation of conidiophore [60][61].

References

  1. Dangl, J.L.; Dietrich, R.A.; Richberg, M.H. Death Don’t Have No Mercy: Cell Death Programs in Plant-Microbe Interactions. Plant Cell 1996, 8, 1793–1807.
  2. Goyet, V.; Billard, E.; Pouvreau, J.B.; Lechat, M.M.; Pelletier, S.; Bahut, M.; Monteau, F.; Spíchal, L.; Delavault, P.; Montiel, G.; et al. Haustorium initiation in the obligate parasitic plant Phelipanche ramosa involves a host-exudated cytokinin signal. J. Exp. Bot. 2017, 68, 5539–5552.
  3. Jones, J.D.; Dangl, J.L. The plant immune system. Nature 2006, 444, 323–329.
  4. Asai, T.; Tena, G.; Plotnikova, J.; Willmann, M.R.; Chiu, W.L.; Gomez-Gomez, L.; Boller, T.; Ausubel, F.M.; Sheen, J. MAP kinase signalling cascade in Arabidopsis innate immunity. Nature 2002, 415, 977–983.
  5. Kaku, H.; Nishizawa, Y.; Ishii-Minami, N.; Akimoto-Tomiyama, C.; Dohmae, N.; Takio, K.; Minami, E.; Shibuya, N. Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc. Natl. Acad. Sci. USA 2006, 103, 11086–11091.
  6. Ausubel, F.M. Are innate immune signaling pathways in plants and animals conserved? Nat. Immunol. 2005, 6, 973–979.
  7. Bolker, M. Sex and crime: Heterotrimeric G proteins in fungal mating and pathogenesis. Fungal Genet. Biol. 1998, 25, 143–156.
  8. Lengeler, K.B.; Davidson, R.C.; D’Souza, C.; Harashima, T.; Shen, W.C.; Wang, P.; Pan, X.; Waugh, M.; Heitman, J. Signal transduction cascades regulating fungal development and virulence. Microbiol. Mol. Biol. Rev. 2000, 64, 746–785.
  9. Yu, J.H. Heterotrimeric G protein signaling and RGSs in Aspergillus nidulans. J. Microbiol. 2006, 44, 145–154.
  10. Regenfelder, E.; Spellig, T.; Hartmann, A.; Lauenstein, S.; Bolker, M.; Kahmann, R. G proteins in Ustilago maydis: Transmission of multiple signals? EMBO J. 1997, 16, 1934–1942.
  11. Muller, P.; Leibbrandt, A.; Teunissen, H.; Cubasch, S.; Aichinger, C.; Kahmann, R. The Gbeta-subunit-encoding gene bpp1 controls cyclic-AMP signaling in Ustilago maydis. Eukaryot. Cell 2004, 3, 806–814.
  12. Liebmann, B.; Gattung, S.; Jahn, B.; Brakhage, A.A. cAMP signaling in Aspergillus fumigatus is involved in the regulation of the virulence gene pksP and in defense against killing by macrophages. Mol. Genet. Genom. 2003, 269, 420–435.
  13. Liebmann, B.; Muller, M.; Braun, A.; Brakhage, A.A. The cyclic AMP-dependent protein kinase a network regulates development and virulence in Aspergillus fumigatus. Infect. Immun. 2004, 72, 5193–5203.
  14. Choi, G.H.; Chen, B.; Nuss, D.L. Virus-mediated or transgenic suppression of a G-protein alpha subunit and attenuation of fungal virulence. Proc. Natl. Acad. Sci. USA 1995, 92, 305–309.
  15. Gao, S.; Nuss, D.L. Distinct roles for two G protein alpha subunits in fungal virulence, morphology, and reproduction revealed by targeted gene disruption. Proc. Natl. Acad. Sci. USA 1996, 93, 14122–14127.
  16. Segers, G.C.; Nuss, D.L. Constitutively activated Galpha negatively regulates virulence, reproduction and hydrophobin gene expression in the chestnut blight fungus Cryphonectria parasitica. Fungal Genet. Biol. 2003, 38, 198–208.
  17. Kasahara, S.; Nuss, D.L. Targeted disruption of a fungal G-protein beta subunit gene results in increased vegetative growth but reduced virulence. Mol. Plant Microbe Interact. 1997, 10, 984–993.
  18. Alspaugh, J.A.; Pukkila-Worley, R.; Harashima, T.; Cavallo, L.M.; Funnell, D.; Cox, G.M.; Perfect, J.R.; Kronstad, J.W.; Heitman, J. Adenylyl cyclase functions downstream of the Galpha protein Gpa1 and controls mating and pathogenicity of Cryptococcus neoformans. Eukaryot. Cell 2002, 1, 75–84.
  19. Xue, C.; Bahn, Y.S.; Cox, G.M.; Heitman, J. G protein-coupled receptor Gpr4 senses amino acids and activates the cAMP-PKA pathway in Cryptococcus neoformans. Mol. Biol. Cell 2006, 17, 667–679.
  20. Wang, P.; Perfect, J.R.; Heitman, J. The G-protein beta subunit GPB1 is required for mating and haploid fruiting in Cryptococcus neoformans. Mol. Cell. Biol. 2000, 20, 352–362.
  21. Madhani, H.D.; Fink, G.R. The riddle of MAP kinase signaling specificity. Trends Genet. 1998, 14, 151–155.
  22. Posas, F.; Takekawa, M.; Saito, H. Signal transduction by MAP kinase cascades in budding yeast. Curr. Opin. Microbiol. 1998, 1, 175–182.
  23. Schaeffer, H.J.; Weber, M.J. Mitogen-activated protein kinases: Specific messages from ubiquitous messengers. Mol. Cell. Biol. 1999, 19, 2435–2444.
  24. Widmann, C.; Gibson, S.; Jarpe, M.B.; Johnson, G.L. Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human. Physiol. Rev. 1999, 79, 143–180.
  25. Romeis, T. Protein kinases in the plant defence response. Curr. Opin. Plant Biol. 2001, 4, 407–414.
  26. Fujimura, M.; Ochiai, N.; Oshima, M.; Motoyama, T.; Ichiishi, A.; Usami, R.; Horikoshi, K.; Yamaguchi, I. Putative homologs of SSK22 MAPKK kinase and PBS2 MAPK kinase of Saccharomyces cerevisiae encoded by os-4 and os-5 genes for osmotic sensitivity and fungicide resistance in Neurospora crassa. Biosci. Biotechnol. Biochem. 2003, 67, 186–191.
  27. Jones, C.A.; Greer-Phillips, S.E.; Borkovich, K.A. The response regulator RRG-1 functions upstream of a mitogen-activated protein kinase pathway impacting asexual development, female fertility, osmotic stress, and fungicide resistance in Neurospora crassa. Mol. Biol. Cell 2007, 18, 2123–2136.
  28. Noguchi, R.; Banno, S.; Ichikawa, R.; Fukumori, F.; Ichiishi, A.; Kimura, M.; Yamaguchi, I.; Fujimura, M. Identification of OS-2 MAP kinase-dependent genes induced in response to osmotic stress, antifungal agent fludioxonil, and heat shock in Neurospora crassa. Fungal Genet. Biol. 2007, 44, 208–218.
  29. Yan, L.; Yang, Q.; Sundin, G.W.; Li, H.; Ma, Z. The mitogen-activated protein kinase kinase BOS5 is involved in regulating vegetative differentiation and virulence in Botrytis cinerea. Fungal Genet. Biol. 2010, 47, 753–760.
  30. Yan, L.; Yang, Q.; Jiang, J.; Michailides, T.J.; Ma, Z. Involvement of a putative response regulator Brrg-1 in the regulation of sporulation, sensitivity to fungicides, and osmotic stress in Botrytis cinerea. Appl. Microbiol. Biotechnol. 2011, 90, 215–226.
  31. Thines, E.; Weber, R.W.; Talbot, N.J. MAP kinase and protein kinase A-dependent mobilization of triacylglycerol and glycogen during appressorium turgor generation by Magnaporthe grisea. Plant Cell 2000, 12, 1703–1718.
  32. Motoyama, T.; Ochiai, N.; Morita, M.; Iida, Y.; Usami, R.; Kudo, T. Involvement of putative response regulator genes of the rice blast fungus Magnaporthe oryzae in osmotic stress response, fungicide action, and pathogenicity. Curr. Genet. 2008, 54, 185–195.
  33. Kawasaki, L.; Sanchez, O.; Shiozaki, K.; Aguirre, J. SakA MAP kinase is involved in stress signal transduction, sexual development and spore viability in Aspergillus nidulans. Mol. Microbiol. 2002, 45, 1153–1163.
  34. Atoui, A.; Bao, D.; Kaur, N.; Grayburn, W.S.; Calvo, A.M. Aspergillus nidulans natural product biosynthesis is regulated by mpkB, a putative pheromone response mitogen-activated protein kinase. Appl. Environ. Microbiol. 2008, 74, 3596–3600.
  35. Bayram, O.; Bayram, O.S.; Ahmed, Y.L.; Maruyama, J.; Valerius, O.; Rizzoli, S.O.; Ficner, R.; Irniger, S.; Braus, G.H. The Aspergillus nidulans MAPK module AnSte11-Ste50-Ste7-Fus3 controls development and secondary metabolism. PLoS Genet. 2012, 8, e1002816.
  36. Xu, J.R.; Hamer, J.E. MAP kinase and cAMP signaling regulate infection structure formation and pathogenic growth in the rice blast fungus Magnaporthe grisea. Genes Dev. 1996, 10, 2696–2706.
  37. Bruno, K.S.; Tenjo, F.; Li, L.; Hamer, J.E.; Xu, J.R. Cellular localization and role of kinase activity of PMK1 in Magnaporthe grisea. Eukaryot. Cell 2004, 3, 1525–1532.
  38. Xu, J.R.; Staiger, C.J.; Hamer, J.E. Inactivation of the mitogen-activated protein kinase Mps1 from the rice blast fungus prevents penetration of host cells but allows activation of plant defense responses. Proc. Natl. Acad. Sci. USA 1998, 95, 12713–12718.
  39. Mey, G.; Held, K.; Scheffer, J.; Tenberge, K.B.; Tudzynski, P. CPMK2, an SLT2-homologous mitogen-activated protein (MAP) kinase, is essential for pathogenesis of Claviceps purpurea on rye: Evidence for a second conserved pathogenesis-related MAP kinase cascade in phytopathogenic fungi. Mol. Microbiol. 2002, 46, 305–318.
  40. Fujioka, T.; Mizutani, O.; Furukawa, K.; Sato, N.; Yoshimi, A.; Yamagata, Y.; Nakajima, T.; Abe, K. MpkA-Dependent and -independent cell wall integrity signaling in Aspergillus nidulans. Eukaryot. Cell 2007, 6, 1497–1510.
  41. Yago, J.I.; Lin, C.H.; Chung, K.R. The SLT2 mitogen-activated protein kinase-mediated signalling pathway governs conidiation, morphogenesis, fungal virulence and production of toxin and melanin in the tangerine pathotype of Alternaria alternata. Mol. Plant Pathol. 2011, 12, 653–665.
  42. Monge, R.A.; Roman, E.; Nombela, C.; Pla, J. The MAP kinase signal transduction network in Candida albicans. Microbiology 2006, 152, 905–912.
  43. Castellanos, M.; Mothi, N.; Munoz, V. Eukaryotic transcription factors can track and control their target genes using DNA antennas. Nat. Commun. 2020, 11, 540.
  44. Tsuji, G.; Kenmochi, Y.; Takano, Y.; Sweigard, J.; Farrall, L.; Furusawa, I.; Horino, O.; Kubo, Y. Novel fungal transcriptional activators, Cmr1p of Colletotrichum lagenarium and pig1p of Magnaporthe grisea, contain Cys2His2 zinc finger and Zn(II)2Cys6 binuclear cluster DNA-binding motifs and regulate transcription of melanin biosynthesis genes in a developmentally specific manner. Mol. Microbiol. 2000, 38, 940–954.
  45. Nikolaev, I.; Cochet, M.F.; Lenouvel, F.; Felenbok, B. A single amino acid, outside the AlcR zinc binuclear cluster, is involved in DNA binding and in transcriptional regulation of the alc genes in Aspergillus nidulans. Mol. Microbiol. 1999, 31, 1115–1124.
  46. Yin, W.B.; Reinke, A.W.; Szilagyi, M.; Emri, T.; Chiang, Y.M.; Keating, A.E.; Pocsi, I.; Wang, C.C.; Keller, N.P. bZIP transcription factors affecting secondary metabolism, sexual development and stress responses in Aspergillus nidulans. Microbiology 2013, 159, 77–88.
  47. Fu, Y.H.; Paietta, J.V.; Mannix, D.G.; Marzluf, G.A. cys-3, the positive-acting sulfur regulatory gene of Neurospora crassa, encodes a protein with a putative leucine zipper DNA-binding element. Mol. Cell. Biol. 1989, 9, 1120–1127.
  48. Tian, C.; Li, J.; Glass, N.L. Exploring the bZIP transcription factor regulatory network in Neurospora crassa. Microbiology 2011, 157, 747–759.
  49. Xiao, P.; Shin, K.S.; Wang, T.; Yu, J.H. Aspergillus fumigatus flbB encodes two basic leucine zipper domain (bZIP) proteins required for proper asexual development and gliotoxin production. Eukaryot. Cell 2010, 9, 1711–1723.
  50. Amich, J.; Schafferer, L.; Haas, H.; Krappmann, S. Regulation of sulphur assimilation is essential for virulence and affects iron homeostasis of the human-pathogenic mould Aspergillus fumigatus. PLoS Pathog. 2013, 9, e1003573.
  51. Montibus, M.; Ducos, C.; Bonnin-Verdal, M.N.; Bormann, J.; Ponts, N.; Richard-Forget, F.; Barreau, C. The bZIP transcription factor Fgap1 mediates oxidative stress response and trichothecene biosynthesis but not virulence in Fusarium graminearum. PLoS ONE 2013, 8, e83377.
  52. Tang, W.; Ru, Y.; Hong, L.; Zhu, Q.; Zuo, R.; Guo, X.; Wang, J.; Zhang, H.; Zheng, X.; Wang, P.; et al. System-wide characterization of bZIP transcription factor proteins involved in infection-related morphogenesis of Magnaporthe oryzae. Environ. Microbiol. 2015, 17, 1377–1396.
  53. Desplan, C.; Theis, J.; O’Farrell, P.H. The sequence specificity of homeodomain-DNA interaction. Cell 1988, 54, 1081–1090.
  54. Kamper, J.; Reichmann, M.; Romeis, T.; Bolker, M.; Kahmann, R. Multiallelic recognition: Nonself-dependent dimerization of the bE and bW homeodomain proteins in Ustilago maydis. Cell 1995, 81, 73–83.
  55. Arnaise, S.; Zickler, D.; Poisier, C.; Debuchy, R. pah1: A homeobox gene involved in hyphal morphology and microconidiogenesis in the filamentous ascomycete Podospora anserina. Mol. Microbiol. 2001, 39, 54–64.
  56. Kim, S.; Park, S.Y.; Kim, K.S.; Rho, H.S.; Chi, M.H.; Choi, J.; Park, J.; Kong, S.; Park, J.; Goh, J.; et al. Homeobox transcription factors are required for conidiation and appressorium development in the rice blast fungus Magnaporthe oryzae. PLoS Genet. 2009, 5, e1000757.
  57. Sun, X.; Zhang, H.; Zhang, Z.; Wang, Y.; Li, S. Involvement of a helix-loop-helix transcription factor CHC-1 in CO(2)-mediated conidiation suppression in Neurospora crassa. Fungal Genet. Biol. 2011, 48, 1077–1086.
  58. Caruso, M.L.; Litzka, O.; Martic, G.; Lottspeich, F.; Brakhage, A.A. Novel basic-region helix-loop-helix transcription factor (AnBH1) of Aspergillus nidulans counteracts the CCAAT-binding complex AnCF in the promoter of a penicillin biosynthesis gene. J. Mol. Biol. 2002, 323, 425–439.
  59. Tuncher, A.; Reinke, H.; Martic, G.; Caruso, M.L.; Brakhage, A.A. A basic-region helix-loop-helix protein-encoding gene (devR) involved in the development of Aspergillus nidulans. Mol. Microbiol. 2004, 52, 227–241.
  60. Jin, F.J.; Nishida, M.; Hara, S.; Koyama, Y. Identification and characterization of a putative basic helix-loop-helix transcription factor involved in the early stage of conidiophore development in Aspergillus oryzae. Fungal Genet. Biol. 2011, 48, 1108–1115.
  61. Jin, F.J.; Takahashi, T.; Matsushima, K.; Hara, S.; Shinohara, Y.; Maruyama, J.; Kitamoto, K.; Koyama, Y. SclR, a basic helix-loop-helix transcription factor, regulates hyphal morphology and promotes sclerotial formation in Aspergillus oryzae. Eukaryot. Cell 2011, 10, 945–955.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license; additional terms may apply. By using this site, you agree to the Terms and Conditions and Privacy Policy.
Upload a video for this entry
Information
Subjects: Microbiology
Contributors MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
jiandong bao
,
Fucheng Lin
,
Lin Li
,
,
Jiaoyu Wang
View Times: 804
Revisions: 4 times (View History)
Update Date: 13 May 2022
Table of Contents
    1000/1000
    Hot Most Recent
    Academic Video Service
    Feedback