Journal of Microbiology

Journal Articles

Genome Sequencing Highlights the Plant Cell Wall Degrading Capacity of Edible Mushroom Stropharia rugosoannulata: Mengpei Guo , Xiaolong Ma , Yan Zhou , Yinbing Bian , Gaolei Liu , Yingli Cai , Tianji Huang , Hongxia Dong , Dingjun Cai , Xueji Wan , Zhihong Wang , Yang Xiao , Heng Kang; J. Microbiol. 2023;61(1):83-93. Published online February 1, 2023; DOI: https://doi.org/10.1007/s12275-022-00003-7

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The basidiomycetous edible mushroom Stropharia rugosoannulata has excellent nutrition, medicine, bioremediation, and biocontrol properties. S. rugosoannulata has been widely and easily cultivated using agricultural by-products showing strong lignocellulose degradation capacity. However, the unavailable high-quality genome information has hindered the research on gene function and molecular breeding of S. rugosoannulata. This study provided a high-quality genome assembly and annotation from S. rugosoannulata monokaryotic strain QGU27 based on combined Illumina-Nanopore data. The genome size was about 47.97 Mb and consisted of 20 scaffolds, with an N50 of 3.73 Mb and a GC content of 47.9%. The repetitive sequences accounted for 17.41% of the genome, mostly long terminal repeats (LTRs). A total of 15,726 coding gene sequences were putatively identified with the BUSCO score of 98.7%. There are 142 genes encoding plant cell wall degrading enzymes (PCWDEs) in the genome, and 52, 39, 30, 11, 8, and 2 genes related to lignin, cellulose, hemicellulose, pectin, chitin, and cutin degradation, respectively. Comparative genomic analysis revealed that S. rugosoannulata is superior in utilizing aldehyde-containing lignins and is possible to utilize algae during the cultivation.

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Analysis of Gene Regulatory Network and Transcription Factors in Different Tissues of the Stropharia rugosoannulata Fruiting Body
Jia Lu, Jing Yan, Na Lu, Jiling Song, Jiayao Lin, Xiaohua Zhou, Xuebing Ying, Zhen Li, Zufa Zhou, Fangjie Yao
Journal of Fungi.2025; 11(2): 123. CrossRef
Evaluation of Genetic Diversity and Agronomic Traits of Germplasm Resources of Stropharia rugosoannulata
Miao Gu, Qiang Chen, Yan Zhang, Yongchang Zhao, Li Wang, Xiangli Wu, Mengran Zhao, Wei Gao
Horticulturae.2024; 10(3): 213. CrossRef
Molecular Profiling of Rice Straw Degradability Discrepancy in Stropharia rugosoannulata Core Germplasm
Wenbing Gong, Yuyu Zeng, Xinru Li, Zhidong Zhao, Nan Shen, Yan Zhou, Yinbing Bian, Yang Xiao
Journal of Agricultural and Food Chemistry.2024; 72(45): 25379. CrossRef
Genome assembly of M. spongiola and comparative genomics of the genus Morchella provide initial insights into taxonomy and adaptive evolution
Qing Meng, Zhanling Xie, Hongyan Xu, Jing Guo, Qingqing Peng, Yanyan Li, Jiabao Yang, Deyu Dong, Taizhen Gao, Fan Zhang
BMC Genomics.2024;[Epub] CrossRef

[PROTOCOL] Determination of protein phosphorylation by polyacrylamide gel electrophoresis: Chang-Ro Lee , Young-Ha Park , Huitae Min , Yeon-Ran Kim , Yeong-Jae Seok; J. Microbiol. 2019;57(2):93-100. Published online January 31, 2019; DOI: https://doi.org/10.1007/s12275-019-9021-y

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Abstract

Phosphorylation is the most important modification for protein regulation; it controls many signal transduction pathways in all organisms. While several tools to detect phosphorylated proteins have been developed to study a variety of basic cellular processes involving protein phosphorylation, these methods have several limitations. Many proteins exhibit a phosphorylation-dependent electrophoretic mobility shift (PDEMS) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and the molecular mechanism responsible for this phenomenon has been elucidated recently. The method for detecting phosphorylated proteins can be simplified by the application of the PDEMS. Herein, we present a novel simple method to detect protein phosphorylation, which is based on the construction of a variant protein displaying a PDEMS. The PDEMS of proteins is caused by the distribution of negatively charged amino acids around the phosphorylation site, i.e. an electrophoretic mobility shift (EMS)-related motif (ΘX1-3ΘX1-3Θ, where Θ corresponds to an acidic or phosphorylated amino acid and X represents any amino acid). The EMS-related motif can be constructed by the introduction of a negative charge by phosphorylation; it results in the decreased binding of SDS to the proteins, consequently inducing the retardation of the mobility of the protein during SDS-PAGE. Based on these molecular analyses of the PDEMS, a protein with the EMSrelated motif is designed and used to determine the in vivo phosphorylation state of the protein. This method may be used as a general strategy to easily measure the ratio of protein phosphorylation in cells.

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Research Support, Non-U.S. Gov't

Trichoderma reesei Sch9 and Yak1 regulate vegetative growth, conidiation, and stress response and induced cellulase production: Xinxing Lv† , Weixin Zhang† , Guanjun Chen , Weifeng Liu; J. Microbiol. 2015;53(4):236-242. Published online January 31, 2015; DOI: https://doi.org/10.1007/s12275-015-4639-x

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Abstract

Protein kinases are key players in controlling many basic cellular processes in almost all the organisms via mediating signal transduction processes. In the present study, we characterized the cellulolytic Trichoderma reesei orthologs of Saccharomyces cerevisiae Sch9 and Yak1 by sequence alignment and functional analysis. The T. reesei Trsch9Δ and Tryak1Δ mutant strains displayed a decreased growth rate on different carbon sources and produced less conidia. The absence of these two kinases also resulted in different but abnormal polarized apical growth as well as sensitivity to various stresses. In addition, disruption of the genes Trsch9 or Tryak1 resulted in perturbation of cell wall integrity. Interestingly, while the induced production of cellulases was slightly compromised in the Trsch9Δ strain, the extracellular production of cellulases was significantly improved in the absence of Yak1. The results indicate that TrSch9 and TrYak1 play an important role in filamentous growth, stress response and induced production of cellulases in T. reesei.

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Broad Substrate-Specific Phosphorylation Events Are Associated With the Initial Stage of Plant Cell Wall Recognition in Neurospora crassa
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STK-12 acts as a transcriptional brake to control the expression of cellulase-encoding genes in Neurospora crassa
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Journal Article

Porphyromonas gingivalis-Derived Lipopolysaccharide-Mediated Activation of MAPK Signaling Regulates Inflammatory Response and Differentiation in Human Periodontal Ligament Fibroblasts: Taegun Seo , Seho Cha , Tae-Il Kim , Hee-Jung Park , Jeong-Soon Lee , Kyung Mi Woo; J. Microbiol. 2012;50(2):311-319. Published online April 27, 2012; DOI: https://doi.org/10.1007/s12275-012-2146-x

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Abstract

Porphyromonas gingivalis (P.g.), which is a potential pathogen for periodontal diseases, contains lipopolysaccharide (LPS), and this endotoxin stimulates a variety of cellular responses. At present, P.g.-derived LPS-induced cellular responses in human periodontal ligament fibroblasts (PDLFs) are not well characterized. Here, we demonstrate that P.gderived LPS regulates inflammatory responses, apoptosis and differentiation in PDLFs. Interleukin-6 (IL-6) and -8 (IL-8) were effectively upregulated by treatment of P.g.-derived LPS, and we confirmed apoptosis markers including elevated cytochrome c levels, active caspase-3 and morphological change in the presence of P.g.-derived LPS. Moreover, when PDLFs were cultured with differentiation media, P.g.- derived LPS reduced the expression of differentiation marker genes, as well as reducing alkaline phosphatase (ALP) activity and mineralization. P.g.-derived LPS-mediated these cellular responses were effectively abolished by treatment of mitogen-activated protein kinase (MAPK) inhibitors. Taken together, our results suggest that P.g.-derived LPS regulates several cellular responses via activation of MAPK signaling pathways in PDLFs.

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Research Support, Non-U.S. Gov'ts

Kaposi’s Sarcoma-Associated Herpesvirus Viral Protein Kinase Interacts with RNA Helicase A and Regulates Host Gene Expression: Jae Eun Jong , Junsoo Park , Sunmi Kim , Taegun Seo; J. Microbiol. 2010;48(2):206-212. Published online May 1, 2010; DOI: https://doi.org/10.1007/s12275-010-0021-1

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Abstract: RNA helicase A (RHA) containing the DExH motif is a human homolog of maleless protein that regulates expression of genes located in the Drosophila X chromosome during dosage compensation. RHA exerts helicase activity that unwinds double-stranded RNA and DNA to a single-strand form. The protein acts as a bridging factor mediating interactions of CBP/p300 and RNA pol II, and consequently affects gene expression. Kaposi’s sarcoma-associated herpesvirus (KSHV) is a member of the γ-herpesvirus subfamily that causes several disorders. The majority of herpesviruses commonly encode predicted viral protein kinases. KSHV open reading frame 36 (ORF36) codes for protein kinase domains, and functions as a serine/threonine protein kinase. KSHV ORF36 is classified as a late gene, as it is expressed during lytic replication and localized in the nuclei of KSHV-infected cells. Recent studies show that viral protein kinase (vPK) interacts with cellular proteins. In this study, we determined the cellular localization of vPK in KSHVinfected BCBL-1 cells using confocal microscopy. Proteomic analysis indicates that cellular proteins interacted with vPK, and co-immunoprecipitation reactions further reveal interactions between vPK and RHA. Moreover, KSHV vPK appeared to regulate the transcriptional activation of Cre promoter, and plays an important role in cellular transcription of RHA.

Ligand-Receptor Recognition for Activation of Quorum Sensing in Staphylococcus aureus: Li-Chun Chen , Li-Tse Tsou , Feng-Jui Chen; J. Microbiol. 2009;47(5):572-581. Published online October 24, 2009; DOI: https://doi.org/10.1007/s12275-009-0004-2

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Abstract: The accessory gene regulator (agr) locus controls many of the virulence toxins involved in Staphylococcus aureus pathogenesis, and can be divided into four specificity groups. AgrC is the only group-specific receptor to mediate both intra-group activation and inter-group inhibition. We studied the ligand-receptor recognition of the agr system in depth by using a luciferase reporter system to identify the key residues responsible for AgrC activation in two closely related agr groups, AgrC-I, and AgrC-IV. Fusion PCR and site-directed mutagenesis were used to screen for functional residues of AgrC. Our data suggest that for AgrC-IV activation, residue 101 is critical for activating the receptor. In contrast, the key residues for the activation of AgrC-I are located at residues 49~59, 107, and 116. However, three residue changes, T101A, V107S, I116S, are sufficient to convert the AIP recognizing specificity from AgrC-IV to AgrC-I.

Molecular Cloning and Nucleotide sequence of Schizosaccharomyces pombe Homologue of the Receptor for Activated Protein Kinase C Gene: Park, Seung Kiel , Yoo, Hyang Sook; J. Microbiol. 1995;33(2):128-131.

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Abstract: Using differential hybridization, we selected the prk gene fortuitously from Schizosaccharomyces pombe homologous to RACK1 of rat which encodes the receptor for activated protein kinase C. The cDNA sequence of prk was determined and its deduced amino acid sequence was 76% homologous to RACK1 and had the feature of trimeric G protein beta subunit. The specific amino acid sequences required for the protein kinase C binding were also present in Prk as in the case of RACK1 protein. From these similarities, we suggest that the Prk is protein kinase C binding protein of S. prombe. The involvement of Prk in signal transduction mediated by protein kinase C remained to be studied.

Isolation and Characterization of Fatty Acid Derivatives from an Actinomycetes and Examination of the Effects on Activities of Phospholipase C and Protein Kinase C: Ko, Hack Ryong , Kim, Bo Yeon , Lee, Hyun Sun , Kang, Dae Ook , Ryu, Sung Ho , Suh, Pann Ghill , Mheen, Tae Ick , Ahnm Jong Seog; J. Microbiol. 1998;36(4):316-321.

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Abstract: In our screening to search inhibitors of phosphoinositide(PI)-specific phospholipase C (PI-PLC), two inhibitors, MT965-A and-B were isolated from a culture broth of an actinomycetes. MT965-A and-B were identified as fatty acid deribatives, 14-methylpentadecanoic acid and 16-methyllinoleic acid methyl ester, respectively, based on the spectral data including NMR and MS. Both inhibitors directly inhibited not only in vitro PLCγ1 activity but also the platelet-derived growth factor(PDGF)-induced inositol phosphates(IPt) formation in NIH 3T3γ1 cells ocerexpressing PLCγ1. However, the inhibitors enhanced in vitro protein kinase C (PKC) activity. On examination of the effects of various fatty acids(FAs) on activities of PLC, PKC, and PDGF-induced IPt formation, the unsaturated FAs(UFAs) showed the same activities like the inhibitors, but the saturated FAs(SFAs) did not show similar activities. It was inferred that the chain length, degree of unsaturation, methyl esterification, branching with a methyl group, and cis-configuration were important for their activity.

Purification and Properties of Novel Calcium-binding Proteins from Streptomyces coelicolor: Chang, Ji Hun , Yoon, Soon Sang , Lhee, Sang Moon , Park, I Ha , Jung, Do Young , Park, Yong Sik , Yim, Jeong Bin; J. Microbiol. 1999;37(1):21-26.

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Abstract: Two novel calcium-binding proteins, named CAB-I and CAB-II, have been isolated from Streptomyces coelicolor. Purification of the calcium-binding proteins involved heat treatment, fractionation with ammonium sulfate, acid treatment, anion exchange and hydrophobic interaction column chromatography, FPLC gel filtration, and preparative isoelectric focusing. A chelex competitive assay and ^45Ca autoradiography verified the calcium-binding ability of the proteins. The major band CAB-II has an apparent molecular weight of 26,000 determined by SDS-polyacrylamide gel electrophoresis and 340,000 determined by gel filtration. The isoelectric point of this molecule showed the acidic nature of the molecule. N-terminal amino acid sequence analysis shows homology to rat Ca^2+/calmodulin-dependent protein kinase-II (CAB-II) and yeast phosphoprotein phosphatase (CAB-I).

A Ser/Thr Specific Protein Kinase Activates the Mouse Rantes Gene after Lipopolysaccharide Stimulation: Youn- Uck Kim , Youn-Hwoan Kim , Duek-Jun An , Hyuk-Chu Kwon; J. Microbiol. 2001;39(4):314-320.

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Abstract: Macrophages stimulated by lipopolysaccharide (LPS) from gram negative bacteria undergo activation of a group of immediate early genes including Rantes. The mouse Rantes gene promoter region contains an LPS responsive element (LRE). We detected 3 specific bands, termed B1, B2, and B3, formed by the interaction of the LRE and proteins found in LPS-stimulated RAW 264.7 cells. An additional band, B4, was determined to be an AP-1 binding protein. The B1 band appears within 1 hour of LPS stimulation. The observed binding pattern could be changed by a specific heparin column fraction of nuclear extracts from LPS-stimulated cells. We have determined that a Ser/Thr-specific protein kinase is activated by LPS stimulation, and this protein kinase enhances B1 band formation. The B1 band can be converted to band B2/B3 by adding specific heparin column fraction. Purified Ser/Thr-specific protein phosphatases PP-1 and PP-2A can stimulate the same conversion to about the same extent. Thus, the formation of the LRE sequence binding complex appears to be regulated by Ser/Thr protein kinase and one or more Ser/Thr specific phosphatases. At least four proteins are involved in the regulation of the LRE-dependent Rantes expression: two binding factors that bind directly to the target sequences, and two factors that control their binding. The future purification and characterization of these binding proteins will reveal in detail the mechanism of Rantes gene activation after LPS stimulation.

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