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- Crystal Structures of Plk1 Polo‑Box Domain Bound to the Human Papillomavirus Minor Capsid Protein L2‑Derived Peptide
- Sujin Jung , Hye Seon Lee , Ho-Chul Shin , Joon Sig Choi , Seung Jun Kim , Bonsu Ku
- J. Microbiol. 2023;61(8):755-764. Published online September 8, 2023
- DOI: https://doi.org/10.1007/s12275-023-00071-3
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Abstract
- Human papillomaviruses (HPVs) can increase the proliferation of infected cells during HPV-driven abnormalities, such as cervical cancer or benign warts. To date, more than 200 HPV genotypes have been identified, most of which are classified into three major genera: Alphapapillomavirus, Betapapillomavirus, and Gammapapillomavirus. HPV genomes commonly encode two structural (L1 and L2) and seven functional (E1, E2, E4–E7, and E8) proteins. L2, the minor structural protein of HPVs, not only serves as a viral capsid component but also interacts with various human proteins during viral infection. A recent report revealed that L2 of HPV16 recruits polo-like kinase 1 (Plk1), a master regulator of eukaryotic mitosis and cell cycle progression, for the delivery of viral DNA to mitotic chromatin during HPV16 infection. In this study, we verified the direct and potent interactions between the polo-box domain (PBD) of Plk1 and PBD-binding motif (S–S–pT–P)-containing phosphopeptides derived from L2 of HPV16/HPV18 (high-risk alphapapillomaviruses), HPV5b (low-risk betapapillomavirus), and HPV4 (low-risk gammapapillomavirus). Subsequent structural determination of the Plk1 PBD bound to the HPV18 or HPV4 L2-derived phosphopeptide demonstrated that they interact with each other in a canonical manner, in which electrostatic interactions and hydrogen bonds play key roles in sustaining the complex. Therefore, our structural and biochemical data imply that Plk1 is a broad binding target of L2 of various HPV genotypes belonging to the Alpha-, Beta-, and Gammapapillomavirus genera.
- Improved tolerance of recombinant Chlamydomonas rainhardtii with putative 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase from Pyropia yezoensis to nitrogen starvation
- Seo-jeong Park , Joon Woo Ahn , Jong-il Choi
- J. Microbiol. 2022;60(1):63-69. Published online December 29, 2021
- DOI: https://doi.org/10.1007/s12275-022-1491-7
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Abstract
- In a previous study, a putative 2-amino-3-carboxymuconate-
6-semialdehyde decarboxylase (ACMSD) was highly expressed
in a mutant strain of Pyropia yezoensis, which exhibited an
improved growth rate compared to its wild strain. To investigate
the functional role of the putative ACMSD (Pyacmsd)
of P. yezoensis, the putative Pyacmsd was cloned and expressed
in Chlamydomonas reinhardtii. Recombinant C. reinhardtii
cells with Pyacmsd (Cr_Pyacmsd) exhibited enhanced tolerance
compared to control C. reinhardtii cells (Cr_control)
under nitrogen starvation. Notably, Cr_Pyacmsd cells showed
accumulation of lipids in nitrogen-enriched conditions. These
results
demonstrate the role of Pyacmsd in the generation of acetyl-coenzyme A. Thus, it can be used to enhance the production of biofuel using microalgae such as C. reinhardtii and increase the tolerance of other biological systems to nitrogendeficient conditions.
Research Support, Non-U.S. Gov't
- Identification of Genes for Mycothiol Biosynthesis in Streptomyces coelicolor A3(2)
- Joo-Hong Park , Chang-Jun Cha , Jung-Hye Roe
- J. Microbiol. 2006;44(1):121-125.
- DOI: https://doi.org/2327 [pii]
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Abstract
- Mycothiol is a low molecular weight thiol compound produced by a number of actinomycetes, and has been suggested to serve both anti-oxidative and detoxifying roles. To investigate the metabolism and the role of mycothiol in Streptomyces coelicolor, the biosynthetic genes (mshA, B, C, and D) were predicted based on sequence homology with the mycobacterial genes and confirmed experimentally. Disruption of the mshA, C, and D genes by PCR targeting mutagenesis resulted in no synthesis of mycothiol, whereas the mshB mutation reduced its level to about 10% of the wild type. The results indicate that the mshA, C, and D genes encode non-redundant biosynthetic enzymes, whereas the enzymatic activity of MshB (acetylase) is shared by at least one other gene product, most likely the mca gene product (amidase).
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