MSK
Search
- Page Path
- HOME > Search
Journal Articles
- Tubulysin Production by the Dead Cells of Archangium gephyra KYC5002
- Seohui Park, Chaehyeon Park, Yujin Ka, Kyungyun Cho
- J. Microbiol. 2024;62(6):463-471. Published online June 13, 2024
- DOI: https://doi.org/10.1007/s12275-024-00130-3
- 32 View
- 0 Download
-
Abstract
- Archangium gephyra KYC5002 produces tubulysins during the death phase. In this study, we aimed to determine whether dead cells produce tubulysins. Cells were cultured for three days until the verge of the death phase, disrupted via ultrasonication, incubated for 2 h, and examined for tubulysin production. Non-disrupted cells produced 0.14 mg/L of tubulysin A and 0.11 mg/L of tubulysin B. Notably, tubulysin A production was increased by 4.4-fold to 0.62 mg/L and that of tubulysin B was increased by 6.7-fold to 0.74 mg/L in the disrupted cells. The same increase in tubulysin production was observed when the cells were killed by adding hydrogen peroxide. However, when the enzymes were inactivated via heat treatment of the cultures at 65 °C for 30 min, no significant increase in tubulysin production due to cell death was observed. Reverse transcription-quantitative polymerase chain reaction analysis of tubB mRNA revealed that the expression levels of tubulysin biosynthetic enzyme genes increased during the death phase compared to those during the vegetative growth phase. Our findings suggest that A. gephyra produces biosynthetic enzymes and subsequently uses them for tubulysin production in the cell death phase or during cell lysis by predators.
- Gene deletion and constitutive expression of the pectate lyase gene 1 (MoPL1) lead to diminished virulence of Magnaporthe oryzae
- Alex Wegner , Florencia Casanova , Marco Loehrer , Angelina Jordine , Stefan Bohnert , Xinyu Liu , Zhengguang Zhang , Ulrich Schaffrath
- J. Microbiol. 2022;60(1):79-88. Published online December 29, 2021
- DOI: https://doi.org/10.1007/s12275-022-1074-7
- 31 View
- 0 Download
- 13 Web of Science
- 11 Crossref
-
Abstract
- Phytopathogenic fungi are known to secrete specific proteins which act as virulence factors and promote host colonization. Some of them are enzymes with plant cell wall degradation capability, like pectate lyases (Pls). In this work, we examined the involvement of Pls in the infection process of Magnaporthe oryzae, the causal agent of rice blast disease. From three Plgenes annotated in the M. oryzae genome, only transcripts of MoPL1 considerably accumulated during the infection process with a peak at 72 h post inoculation. Both, gene deletion and a constitutive expression of MoPL1 in M. oryzae led to a significant reduction in virulence. By contrast, mutants that constitutively expressed an enzymatic inactive version of MoPl1 did not differ in virulence compared to the wild type isolate. This indicates that the enzymatic activity of MoPl1 is responsible for diminished virulence, which is presumably due to degradation products recognized as danger associated molecular patterns (DAMPs), which strengthen the plant immune response. Microscopic analysis of infection sites pointed to an increased plant defense response. Additionally, MoPl1 tagged with mRFP, and not the enzymatic inactive version, focally accumulated in attacked plant cells beneath appressoria and at sites where fungal hyphae transverse from one to another cell. These findings shed new light on the role of pectate lyases during tissue colonization in the necrotrophic stage of M. oryzae's life cycle.
-
Citations
Citations to this article as recorded by
- Fusarium sacchari FsNis1 induces plant immunity
Ruolin Di, Lixiang Zhu, Zhen Huang, Minyan Lu, Liuyu Yin, Caixia Wang, Yixue Bao, Zhenzhen Duan, Charles A. Powell, Qin Hu, Jisen Zhang, Muqing Zhang, Wei Yao
Gene.2024; 907: 148260. CrossRef - Litchi aspartic protease LcAP1 enhances plant resistance via suppressing cell death triggered by the pectate lyase PlPeL8 from Peronophythora litchii
Wen Li, Peng Li, Yizhen Deng, Zijing Zhang, Junjian Situ, Ji Huang, Minhui Li, Pinggen Xi, Zide Jiang, Guanghui Kong
New Phytologist.2024; 242(6): 2682. CrossRef - Unravelling transcriptional responses of the willow to Fusarium kuroshium infection
Enrique Ibarra-Laclette, Luis A. Martínez-Rodríguez, Eric E. Hernández-Domínguez, Mizraim Olivares-Miranda, Benjamín Rodríguez-Haas, Emanuel Villafán, Claudia-Anahí Pérez-Torres, Diana Sánchez-Rangel
Physiological and Molecular Plant Pathology.2024; 133: 102379. CrossRef - Recognition of the inducible, secretory small protein OsSSP1 by the membrane receptor OsSSR1 and the co-receptor OsBAK1 confers rice resistance to the blast fungus
Tianfeng Zhao, Shijie Ma, Ziying Kong, Haimiao Zhang, Yi Wang, Junzhe Wang, Jiazong Liu, Wanzhen Feng, Tong Liu, Chunyan Liu, Suochen Liang, Shilin Lu, Xinyu Li, Haipeng Zhao, Chongchong Lu, Muhammad Zunair Latif, Ziyi Yin, Yang Li, Xinhua Ding
Molecular Plant.2024; 17(5): 807. CrossRef - A plant cell death-inducing protein from litchi interacts with Peronophythora litchii pectate lyase and enhances plant resistance
Wen Li, Peng Li, Yizhen Deng, Junjian Situ, Zhuoyuan He, Wenzhe Zhou, Minhui Li, Pinggen Xi, Xiangxiu Liang, Guanghui Kong, Zide Jiang
Nature Communications.2024;[Epub] CrossRef - Roles of Three FgPel Genes in the Development and Pathogenicity Regulation of Fusarium graminearum
Lu Cai, Xiao Xu, Ye Dong, Yingying Jin, Younes M. Rashad, Dongfang Ma, Aiguo Gu
Journal of Fungi.2024; 10(10): 666. CrossRef - Pectate Lyase from Fusarium sacchari Induces Plant Immune Responses and Contributes to Virulence
Caixia Wang, Zhen Huang, Zhenzhen Duan, Lixiang Zhu, Ruolin Di, Yixue Bao, Charles A. Powell, Qin Hu, Baoshan Chen, Muqing Zhang, Wei Yao, Lindsey Price Burbank
Microbiology Spectrum.2023;[Epub] CrossRef -
Pectate Lyase Genes Abundantly Expressed During the Infection Regulate Morphological Development of
Colletotrichum camelliae
and
CcPEL16
Is Required for Full Virulence to Tea Plants
Hong Jiang, Qinghai Cao, Xinchao Wang, Wuyun Lv, Yuchun Wang, Aaron P. Mitchell
mSphere.2023;[Epub] CrossRef - Small GTPases RasA and RasB regulate development, patulin production, and virulence of Penicillium expansum
Yuanyuan Zong, Xuemei Zhang, Di Gong, Feng Zhang, Lirong Yu, Yang Bi, Edward Sionov, Dov Prusky
Postharvest Biology and Technology.2023; 197: 112192. CrossRef -
Whole-genome sequencing and comparative genomics reveal the potential pathogenic mechanism of
Neoscytalidium dimidiatum
on pitaya
Meng Wang, Min Xu, Zhouwen Wang, Yi Ding, Shaoling Kang, Senrong Jiang, Shuangshuang Wei, Jun Xie, Jiaquan Huang, Dongdong Li, Wenbin Hu, Hongli Li, Xingyu Jiang, Hua Tang, Yonglin Wang
Microbiology Spectrum.2023;[Epub] CrossRef - Identification of RT-qPCR reference genes suitable for gene function studies in the pitaya canker disease pathogen Neoscytalidium dimidiatum
Meng Wang, Zhouwen Wang, Shuangshuang Wei, Jun Xie, Jiaquan Huang, Dongdong Li, Wenbin Hu, Hongli Li, Hua Tang
Scientific Reports.2022;[Epub] CrossRef
- Fusarium sacchari FsNis1 induces plant immunity
- Adenosylhomocysteinase like 1 interacts with nonstructural 5A and regulates hepatitis C virus propagation
- Yun-Sook Lim , Han N. Mai , Lap P. Nguyen , Sang Min Kang , Dongseob Tark , Soon B. Hwang
- J. Microbiol. 2021;59(1):101-109. Published online December 23, 2020
- DOI: https://doi.org/10.1007/s12275-021-0470-8
- 23 View
- 0 Download
- 3 Web of Science
- 3 Crossref
-
Abstract
- Hepatitis C virus (HCV) life cycle is highly dependent on cellular proteins for viral propagation. In order to identify the cellular factors involved in HCV propagation, we previously performed a protein microarray assay using the HCV nonstructural 5A (NS5A) protein as a probe. Of ~9,000 human cellular proteins immobilized in a microarray, adenosylhomocysteinase like 1 (AHCYL1) was among 90 proteins identified as NS5A interactors. Of these candidates, AHCYL1 was selected for further study. In the present study, we verified the physical interaction between NS5A and AHCYL1 by both in vitro pulldown and coimmunoprecipitation assays. Furthermore, HCV NS5A interacted with endogenous AHCYL1 in Jc1-infected cells. Both NS5A and AHCYL1 were colocalized in the cytoplasmic region in HCV-replicating cells. siRNAmediated knockdown of AHCYL1 abrogated HCV propagation. Exogenous expression of the siRNA-resistant AHCYL1 mutant, but not of the wild-type AHCYL1, restored HCV protein expression levels, indicating that AHCYL1 was required specifically for HCV propagation. Importantly, AHCYL1 was involved in the HCV internal ribosome entry site-mediated translation step of the HCV life cycle. Finally, we demonstrated that the proteasomal degradation pathway of AHCYL1 was modulated by persistent HCV infection. Collectively, these data suggest that HCV may modulate the AHCYL1 protein to promote viral propagation.
-
Citations
Citations to this article as recorded by- Amuvatinib Blocks SARS-CoV-2 Infection at the Entry Step of the Viral Life Cycle
Trang T. X. Huynh, Thuy X. Pham, Gun-Hee Lee, Jae-Bong Lee, Sung-Geun Lee, Dongseob Tark, Yun-Sook Lim, Soon B. Hwang, Donna M. Neumann
Microbiology Spectrum.2023;[Epub] CrossRef - Inhibition of KIF20A suppresses the replication of influenza A virus by inhibiting viral entry
Hoyeon Jeon, Younghyun Lim, In-Gu Lee, Dong-In Kim, Keun Pil Kim, So-Hee Hong, Jeongkyu Kim, Youn-Sang Jung, Young-Jin Seo
Journal of Microbiology.2022; 60(11): 1113. CrossRef - Asunaprevir, a Potent Hepatitis C Virus Protease Inhibitor, Blocks SARS-CoV-2 Propagation
Yun-Sook Lim, Lap P. Nguyen, Gun-Hee Lee, Sung-Geun Lee, Kwang-Soo Lyoo, Bumseok Kim, Soon B. Hwang
Molecules and Cells.2021; 44(9): 688. CrossRef
- Amuvatinib Blocks SARS-CoV-2 Infection at the Entry Step of the Viral Life Cycle
- Mutants defective in the production of encapsulin show a tan-phaselocked phenotype in Myxococcus xanthus
- Dohee Kim , Juo Choi , Sunjin Lee , Hyesook Hyun , Kyoung Lee , Kyungyun Cho
- J. Microbiol. 2019;57(9):795-802. Published online June 11, 2019
- DOI: https://doi.org/10.1007/s12275-019-8683-9
- 22 View
- 0 Download
- 13 Web of Science
- 10 Crossref
-
Abstract
- Myxococcus xanthus, a myxobacterium, displays phase variation between yellow phase and tan phase. We found that deletion of the encA gene encoding encapsulin and the encF gene encoding a metalloprotease causes formation of tan colonies that never transform into yellow colonies. The encA and encF mutants were defective in the production of DKxanthene and myxovirescin. They did not produce extracellular polysaccharides; hence, the cells did not aggregate in liquid and showed reduced swarming on agar plates. The mutants had defective sporulation, but were rescued extracellularly by wild type cells. All these traits indicate that the encA and encF mutants are likely to be tan-phase-locked, and encapsulin has a close relationship with phase variation in M. xanthus. The encA and encF genes are localized in the same gene cluster, encBAEFG (MXAN_3557~MXAN_3553). Unlike the encA and encF genes, deletion of other genes in the cluster did not show tan-phase-locked phenotype.
-
Citations
Citations to this article as recorded by- Encapsulated Ferritin-like Proteins: A Structural Perspective
Elif Eren, Norman R. Watts, Felipe Montecinos, Paul T. Wingfield
Biomolecules.2024; 14(6): 624. CrossRef - A widespread bacterial protein compartment sequesters and stores elemental sulfur
Robert Benisch, Michael P. Andreas, Tobias W. Giessen
Science Advances.2024;[Epub] CrossRef - Structure and heterogeneity of a highly cargo-loaded encapsulin shell
Seokmu Kwon, Michael P. Andreas, Tobias W. Giessen
Journal of Structural Biology.2023; 215(4): 108022. CrossRef - Bacterial Nanocompartments: Structures, Functions, and Applications
Harry Benjamin McDowell, Egbert Hoiczyk, Michael Y. Galperin
Journal of Bacteriology.2022;[Epub] CrossRef - Condensation and Protection of DNA by the Myxococcus xanthus Encapsulin: A Novel Function
Ana V. Almeida, Ana J. Carvalho, Tomás Calmeiro, Nykola C. Jones, Søren V. Hoffmann, Elvira Fortunato, Alice S. Pereira, Pedro Tavares
International Journal of Molecular Sciences.2022; 23(14): 7829. CrossRef - Encapsulins
Tobias W. Giessen
Annual Review of Biochemistry.2022; 91(1): 353. CrossRef - Advances in encapsulin nanocompartment biology and engineering
Jesse A. Jones, Tobias W. Giessen
Biotechnology and Bioengineering.2021; 118(1): 491. CrossRef - Encapsulin nanocages: Protein encapsulation and iron sequestration
Ana V. Almeida, Ana J. Carvalho, Alice S. Pereira
Coordination Chemistry Reviews.2021; 448: 214188. CrossRef - Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism
Robert J Nichols, Benjamin LaFrance, Naiya R Phillips, Devon R Radford, Luke M Oltrogge, Luis E Valentin-Alvarado, Amanda J Bischoff, Eva Nogales, David F Savage
eLife.2021;[Epub] CrossRef - Nanotechnological Applications Based on Bacterial Encapsulins
Javier M. Rodríguez, Carolina Allende-Ballestero, Jeroen J. L. M. Cornelissen, José R. Castón
Nanomaterials.2021; 11(6): 1467. CrossRef
- Encapsulated Ferritin-like Proteins: A Structural Perspective
First
Prev
TOP
