Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress
Profilins (PFNs) are actin monomer-binding proteins that function as antimicrobial agents in plant phloem sap. Although the roles of <i>Arabidopsis thaliana</i> profilin protein isoforms (AtPFNs) in regulating actin polymerization have already been described, their biochemical and molecu...
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MDPI AG
2022-09-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/27/18/5771 |
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| author | Hyosuk Son Young Jun Jung Seong-Cheol Park Il Ryong Kim Joung Hun Park Mi-Kyeong Jang Jung Ro Lee |
| author_facet | Hyosuk Son Young Jun Jung Seong-Cheol Park Il Ryong Kim Joung Hun Park Mi-Kyeong Jang Jung Ro Lee |
| author_sort | Hyosuk Son |
| collection | DOAJ |
| description | Profilins (PFNs) are actin monomer-binding proteins that function as antimicrobial agents in plant phloem sap. Although the roles of <i>Arabidopsis thaliana</i> profilin protein isoforms (AtPFNs) in regulating actin polymerization have already been described, their biochemical and molecular functions remain to be elucidated. Interestingly, a previous study indicated that AtPFN2 with high molecular weight (HMW) complexes showed lower antifungal activity than AtPFN1 with low molecular weight (LMW). These were bacterially expressed and purified to characterize the unknown functions of AtPFNs with different structures. In this study, we found that AtPFN1 and AtPFN2 proteins have LMW and HMW structures, respectively, but only AtPFN2 has a potential function as a molecular chaperone, which has never been reported elsewhere. AtPFN2 has better protein stability than AtPFN1 due to its higher molecular weight under heat shock conditions. The function of AtPFN2 as a holdase chaperone predominated in the HMW complexes, whereas the chaperone function of AtPFN1 was not observed in the LMW forms. These results suggest that AtPFN2 plays a critical role in plant tolerance by increasing hydrophobicity due to external heat stress. |
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| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-09T23:02:43Z |
| publishDate | 2022-09-01 |
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| spelling | doaj.art-21fca56cbc9a4023a9215f9c005171e12023-11-23T17:58:31ZengMDPI AGMolecules1420-30492022-09-012718577110.3390/molecules27185771Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock StressHyosuk Son0Young Jun Jung1Seong-Cheol Park2Il Ryong Kim3Joung Hun Park4Mi-Kyeong Jang5Jung Ro Lee6Department of Polymer Science and Engineering, Sunchon National University, Suncheon 38286, KoreaNational Institute of Ecology (NIE), Seocheon 33657, KoreaDepartment of Polymer Science and Engineering, Sunchon National University, Suncheon 38286, KoreaNational Institute of Ecology (NIE), Seocheon 33657, KoreaDivision of Applied Life Science (BK21+) and PMBBRC, Gyeongsang National University, Jinju 52828, KoreaDepartment of Polymer Science and Engineering, Sunchon National University, Suncheon 38286, KoreaNational Institute of Ecology (NIE), Seocheon 33657, KoreaProfilins (PFNs) are actin monomer-binding proteins that function as antimicrobial agents in plant phloem sap. Although the roles of <i>Arabidopsis thaliana</i> profilin protein isoforms (AtPFNs) in regulating actin polymerization have already been described, their biochemical and molecular functions remain to be elucidated. Interestingly, a previous study indicated that AtPFN2 with high molecular weight (HMW) complexes showed lower antifungal activity than AtPFN1 with low molecular weight (LMW). These were bacterially expressed and purified to characterize the unknown functions of AtPFNs with different structures. In this study, we found that AtPFN1 and AtPFN2 proteins have LMW and HMW structures, respectively, but only AtPFN2 has a potential function as a molecular chaperone, which has never been reported elsewhere. AtPFN2 has better protein stability than AtPFN1 due to its higher molecular weight under heat shock conditions. The function of AtPFN2 as a holdase chaperone predominated in the HMW complexes, whereas the chaperone function of AtPFN1 was not observed in the LMW forms. These results suggest that AtPFN2 plays a critical role in plant tolerance by increasing hydrophobicity due to external heat stress.https://www.mdpi.com/1420-3049/27/18/5771AtPFNprofilinheat shockhigher molecular weightmolecular chaperone |
| spellingShingle | Hyosuk Son Young Jun Jung Seong-Cheol Park Il Ryong Kim Joung Hun Park Mi-Kyeong Jang Jung Ro Lee Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress Molecules AtPFN profilin heat shock higher molecular weight molecular chaperone |
| title | Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress |
| title_full | Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress |
| title_fullStr | Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress |
| title_full_unstemmed | Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress |
| title_short | Functional Characterization of an <i>Arabidopsis</i> Profilin Protein as a Molecular Chaperone under Heat Shock Stress |
| title_sort | functional characterization of an i arabidopsis i profilin protein as a molecular chaperone under heat shock stress |
| topic | AtPFN profilin heat shock higher molecular weight molecular chaperone |
| url | https://www.mdpi.com/1420-3049/27/18/5771 |
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