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Jin Park 1 Article
Gly184 of the Escherichia coli cAMP receptor protein provides optimal context for both DNA binding and RNA polymerase interaction
Matt N. Hicks , Sanjiva Gunasekara , Jose Serate , Jin Park , Pegah Mosharaf , Yue Zhou , Jin-Won Lee , Hwan Youn
J. Microbiol. 2017;55(10):816-822.   Published online September 28, 2017
DOI: https://doi.org/10.1007/s12275-017-7266-x
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AbstractAbstract PDF
The Escherichia coli cAMP receptor protein (CRP) utilizes the helix-turn-helix motif for DNA binding. The CRP’s recognition helix, termed F-helix, includes a stretch of six amino acids (Arg180, Glu181, Thr182, Val183, Gly184, and Arg185) for direct DNA contacts. Arg180, Glu181 and Arg185 are known as important residues for DNA binding and specificity, but little has been studied for the other residues. Here we show that Gly184 is another F-helix residue critical for the transcriptional activation function of CRP. First, glycine was repeatedly selected at CRP position 184 for its unique ability to provide wild type-level transcriptional activation activity. To dissect the glycine requirement, wild type CRP and mutants G184A, G184F, G184S, and G184Y were purified and their in vitro DNA-binding activity was measured. G184A and G184F displayed reduced DNA binding, which may explain their low transcriptional activation activity. However, G184S and G184Y displayed apparently normal DNA affinity. Therefore, an additional factor is needed to account for the diminished transcriptional activation function in G184S and G184Y, and the best explanation is perturbations in their interaction with RNA polymerase. The fact that glycine is the smallest amino acid could not fully warrant its suitability, as shown in this study. We hypothesize that Gly184 fulfills the dual functions of DNA binding and RNA polymerase interaction by conferring conformational flexibility to the F-helix.

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Citations to this article as recorded by  
  • cAMP-independent DNA binding of the CRP family protein DdrI from Deinococcus radiodurans
    Yudong Wang, Jing Hu, Xufan Gao, Yuchen Cao, Shumai Ye, Cheng Chen, Liangyan Wang, Hong Xu, Miao Guo, Dong Zhang, Ruhong Zhou, Yuejin Hua, Ye Zhao, Paul Babitzke
    mBio.2024;[Epub]     CrossRef
  • Unexpected Requirement of Small Amino Acids at Position 183 for DNA Binding in the Escherichia coli cAMP Receptor Protein
    Marcus Carranza, Amanda Rea, Daisy Pacheco, Christian Montiel, Jin Park, Hwan Youn
    Journal of Microbiology.2024; 62(10): 871.     CrossRef
  • cAMP Activation of the cAMP Receptor Protein, a Model Bacterial Transcription Factor
    Hwan Youn, Marcus Carranza
    Journal of Microbiology.2023; 61(3): 277.     CrossRef
Jin Park 3 Articles
SimpleMicrobiome: An integrated web-based platform for streamlined microbiome data analysis and visualization
Seong-In Na, Juhee Kim, So-Yeon Kim, Jin Park, Yong-Joon Cho
J. Microbiol. 2026;64(9):e2606011.   Published online September 18, 2026
DOI: https://doi.org/10.71150/jm.2606011
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AbstractAbstract PDFSupplementary Material

Microbiome studies require multiple analytical steps after initial sequence processing. These steps commonly include data harmonization, preprocessing, taxonomic profiling, diversity analysis, differential abundance testing, predictive modeling, network inference, and preparation of publication-ready outputs. Although robust packages are available for many of these tasks, routine use often depends on command-line workflows, repeated data reformatting, and method-specific scripting. These requirements can limit accessibility for experimental researchers and complicate consistent analysis across interdisciplinary teams. We developed SimpleMicrobiome, a web-based R Shiny platform that integrates established microbiome analysis methods into a single interactive downstream workflow. The application accepts standard abundance, taxonomy, and metadata tables, supports interactive preprocessing and sample filtering, and provides modules for taxa profile visualization, alpha and beta diversity analysis, ANCOM-BC2 and MaAsLin2 differential abundance testing, Random Forest modeling with SHAP-based interpretation, microbial association network inference using SparCC and SPIEC-EASI through NetCoMi, correlation heatmaps, and dbRDA/CAP-style association biplots. The platform is implemented as a modular Shiny application so that preprocessing choices are propagated across downstream analyses, results can be exported as figures and tables, and the same application can be run through the public server, source-code installation, or a Docker image.

SimpleMicrobiome consolidates major downstream microbiome analysis tasks in an accessible browser-based environment while retaining links to established analytical frameworks. The platform may reduce technical barriers for non-programming users, improve consistency across exploratory and reporting-oriented analyses, and support collaborative microbiome research. The public application is available at https://simplemicrobiome.mglab.org, the source code is available at https://github.com/yjcho2252/SimpleMicrobiome, and a Docker image for local deployment is available at https://hub.docker.com/r/mglab2252/simplemicrobiome.

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  • Effect of a potassium-competitive acid blocker on the gut microbiota in patients undergoing percutaneous coronary intervention: a randomized pilot study
    Sang Hoon Lee, Seong-In Na, Sung Chul Park, Byung Ryul Cho, Bong Ki Lee, Yong-Joon Cho, Hyunseok Cho, Hee-Jeong Youk, Dong Ryeol Ryu
    Frontiers in Cellular and Infection Microbiology.2026;[Epub]     CrossRef
Erratum: Unexpected Requirement of Small Amino Acids at Position 183 for DNA Binding in the Escherichia coli cAMP Receptor Protein
Marcus Carranza, Amanda Rea, Daisy Pacheco, Christian Montiel, Jin Park, Hwan Youn
J. Microbiol. 2024;62(12):1177-1177.   Published online November 6, 2024
DOI: https://doi.org/10.1007/s12275-024-00189-y
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Unexpected Requirement of Small Amino Acids at Position 183 for DNA Binding in the Escherichia coli cAMP Receptor Protein
Marcus Carranza, Amanda Rea, Daisy Pacheco, Christian Montiel, Jin Park, Hwan Youn
J. Microbiol. 2024;62(10):871-882.   Published online September 6, 2024
DOI: https://doi.org/10.1007/s12275-024-00169-2
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  • 14 Download
  • 5 Web of Science
  • 3 Crossref
AbstractAbstract PDF
The Escherichia coli cAMP receptor protein (CRP) relies on the F-helix, the recognition helix of the helix-turn-helix motif, for DNA binding. The importance of the CRP F-helix in DNA binding is well-established, yet there is little information on the roles of its non-base-contacting residues. Here, we show that a CRP F-helix position occupied by a non-base-contacting residue Val183 bears an unexpected importance in DNA binding. Codon randomization and successive in vivo screening selected six amino acids (alanine, cysteine, glycine, serine, threonine, and valine) at CRP position 183 to be compatible with DNA binding. These amino acids are quite different in their amino acid properties (polar, non-polar, hydrophobicity), but one commonality is that they are all relatively small. Larger amino acid substitutions such as histidine, methionine, and tyrosine were made site-directedly and showed to have no detectable DNA binding, further supporting the requirement of small amino acids at CRP position 183. Bioinformatics analysis revealed that small amino acids (92.15% valine and 7.75% alanine) exclusively occupy the position analogous to CRP Val183 in 1,007 core CRP homologs, consistent with our mutant data. However, in extended CRP homologs comprising 3700 proteins, larger amino acids could also occupy the position analogous to CRP Val183 albeit with low occurrence. Another bioinformatics analysis suggested that large amino acids could be tolerated by compensatory small-sized amino acids at their neighboring positions. A full understanding of the unexpected requirement of small amino acids at CRP position 183 for DNA binding entails the verification of the hypothesized compensatory change(s) in CRP.

Citations

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  • Adaptive evolution resulted in three subtypes of the Riemerella anatipestifer crpR1 gene
    Jialing Wang, Xiaoli Du, Hui Yin, Xiaoying Zhang, Shiqi Wang, Hongyan Liao, Xingyu Zhang, Yuting Zheng, Qinghai Hu
    Journal of Bacteriology.2026;[Epub]     CrossRef
  • The OsMYB4 transcription factor enables coordinated improvement of grain yield and quality in rice
    Huan Xu, Erchao Duan, Qingkai Wang, Rongbo Chen, Chuanwei Gu, Yipeng Zhang, Wenjing Zhang, Rushuang Zhang, Rongxin Tao, Yunpeng Zhang, Wenting Lv, Jiajia Chi, Huimin Zhai, Zhihao Qiao, Zhuo Chen, Xuan Teng, Yunlu Tian, Shijia Liu, Xi Liu, Ling Jiang, Yuqi
    Nature Communications.2026;[Epub]     CrossRef
  • SPD_0410 negatively regulates capsule polysaccharide synthesis and virulence in Streptococcus pneumoniae D39
    Ye Tao, Li Lei, Shuhui Wang, Xuemei Zhang, Yibing Yin, Yuqiang Zheng
    Frontiers in Microbiology.2025;[Epub]     CrossRef

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