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Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity

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Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity. / Ling, M. L.; Wex, H.; Grawe, S.; Jakobsson, J.; Londahl, J.; Hartmann, S.; Finster, K.; Boesen, T.; Santl-Temkiv, T.

I: Journal of Geophysical Research, Bind 123, Nr. 3, 16.02.2018, s. 1802-1810.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Ling, ML, Wex, H, Grawe, S, Jakobsson, J, Londahl, J, Hartmann, S, Finster, K, Boesen, T & Santl-Temkiv, T 2018, 'Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity', Journal of Geophysical Research, bind 123, nr. 3, s. 1802-1810. https://doi.org/10.1002/2017JD027307

APA

Ling, M. L., Wex, H., Grawe, S., Jakobsson, J., Londahl, J., Hartmann, S., Finster, K., Boesen, T., & Santl-Temkiv, T. (2018). Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity. Journal of Geophysical Research, 123(3), 1802-1810. https://doi.org/10.1002/2017JD027307

CBE

Ling ML, Wex H, Grawe S, Jakobsson J, Londahl J, Hartmann S, Finster K, Boesen T, Santl-Temkiv T. 2018. Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity. Journal of Geophysical Research. 123(3):1802-1810. https://doi.org/10.1002/2017JD027307

MLA

Vancouver

Ling ML, Wex H, Grawe S, Jakobsson J, Londahl J, Hartmann S o.a. Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity. Journal of Geophysical Research. 2018 feb 16;123(3):1802-1810. https://doi.org/10.1002/2017JD027307

Author

Ling, M. L. ; Wex, H. ; Grawe, S. ; Jakobsson, J. ; Londahl, J. ; Hartmann, S. ; Finster, K. ; Boesen, T. ; Santl-Temkiv, T. / Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity. I: Journal of Geophysical Research. 2018 ; Bind 123, Nr. 3. s. 1802-1810.

Bibtex

@article{6c68b114b5cc49efa9f8ea7875d86bad,
title = "Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity",
abstract = "Ice nucleation active bacteria have attracted particular attention due to their unique ability to produce specific ice nucleation proteins (INpros), which are the most efficient ice nuclei known as they induce nucleation at temperatures close to 0 degrees C. Our model bacterium Pseudomonas syringae strain R10.79 produced INpros containing 67 tandem repeats, forming the proposed ice-binding surface. To understand the role of the INpro repeats as well as the role of intermolecular interactions between INpros for their ice nucleation behavior, we produced a truncated version of the protein with only 16 tandem repeats (INpro(16R)). The purified INpro(16R) produced oligomers of varying sizes. Immersion freezing ice nucleation behavior of purified INpro(16R) was characterized by droplet-freezing assays and in the Leipzig Aerosol Cloud Interaction Simulator. Predominant INpro(16R) oligomers introduced into Leipzig Aerosol Cloud Interaction Simulator as single particles with diameters of 50nm or 70nm were ice nucleation active at temperatures of -26 degrees C and -24 degrees C, respectively. These are much lower temperatures compared to that of intact INpros (-12 degrees C). The data clearly indicated that the number of repeats determines the ice nucleation temperature. In addition, ice nucleation between -9 degrees C and -10 degrees C, comparable to the activity of intact INpro, was caused by higher-order INpro(16R) oligomers. This supported previous observations that INpro oligomerization increases the ice-binding surface, thereby affecting ice nucleation activity. In conclusion, both repeat number and oligomerization contribute in a seemingly independent manner to the nucleation mechanism of INpros.",
keywords = "precipitation, bioaerosols, PSEUDOMONAS-SYRINGAE, BACTERIA, PRECIPITATION, NUCLEI, PLANTS, IMPACT, MODEL",
author = "Ling, {M. L.} and H. Wex and S. Grawe and J. Jakobsson and J. Londahl and S. Hartmann and K. Finster and T. Boesen and T. Santl-Temkiv",
year = "2018",
month = feb,
day = "16",
doi = "10.1002/2017JD027307",
language = "English",
volume = "123",
pages = "1802--1810",
journal = "Journal of Geophysical Research",
issn = "0148-0227",
publisher = "American Geophysical Union",
number = "3",

}

RIS

TY - JOUR

T1 - Effects of Ice Nucleation Protein Repeat Number and Oligomerization Level on Ice Nucleation Activity

AU - Ling, M. L.

AU - Wex, H.

AU - Grawe, S.

AU - Jakobsson, J.

AU - Londahl, J.

AU - Hartmann, S.

AU - Finster, K.

AU - Boesen, T.

AU - Santl-Temkiv, T.

PY - 2018/2/16

Y1 - 2018/2/16

N2 - Ice nucleation active bacteria have attracted particular attention due to their unique ability to produce specific ice nucleation proteins (INpros), which are the most efficient ice nuclei known as they induce nucleation at temperatures close to 0 degrees C. Our model bacterium Pseudomonas syringae strain R10.79 produced INpros containing 67 tandem repeats, forming the proposed ice-binding surface. To understand the role of the INpro repeats as well as the role of intermolecular interactions between INpros for their ice nucleation behavior, we produced a truncated version of the protein with only 16 tandem repeats (INpro(16R)). The purified INpro(16R) produced oligomers of varying sizes. Immersion freezing ice nucleation behavior of purified INpro(16R) was characterized by droplet-freezing assays and in the Leipzig Aerosol Cloud Interaction Simulator. Predominant INpro(16R) oligomers introduced into Leipzig Aerosol Cloud Interaction Simulator as single particles with diameters of 50nm or 70nm were ice nucleation active at temperatures of -26 degrees C and -24 degrees C, respectively. These are much lower temperatures compared to that of intact INpros (-12 degrees C). The data clearly indicated that the number of repeats determines the ice nucleation temperature. In addition, ice nucleation between -9 degrees C and -10 degrees C, comparable to the activity of intact INpro, was caused by higher-order INpro(16R) oligomers. This supported previous observations that INpro oligomerization increases the ice-binding surface, thereby affecting ice nucleation activity. In conclusion, both repeat number and oligomerization contribute in a seemingly independent manner to the nucleation mechanism of INpros.

AB - Ice nucleation active bacteria have attracted particular attention due to their unique ability to produce specific ice nucleation proteins (INpros), which are the most efficient ice nuclei known as they induce nucleation at temperatures close to 0 degrees C. Our model bacterium Pseudomonas syringae strain R10.79 produced INpros containing 67 tandem repeats, forming the proposed ice-binding surface. To understand the role of the INpro repeats as well as the role of intermolecular interactions between INpros for their ice nucleation behavior, we produced a truncated version of the protein with only 16 tandem repeats (INpro(16R)). The purified INpro(16R) produced oligomers of varying sizes. Immersion freezing ice nucleation behavior of purified INpro(16R) was characterized by droplet-freezing assays and in the Leipzig Aerosol Cloud Interaction Simulator. Predominant INpro(16R) oligomers introduced into Leipzig Aerosol Cloud Interaction Simulator as single particles with diameters of 50nm or 70nm were ice nucleation active at temperatures of -26 degrees C and -24 degrees C, respectively. These are much lower temperatures compared to that of intact INpros (-12 degrees C). The data clearly indicated that the number of repeats determines the ice nucleation temperature. In addition, ice nucleation between -9 degrees C and -10 degrees C, comparable to the activity of intact INpro, was caused by higher-order INpro(16R) oligomers. This supported previous observations that INpro oligomerization increases the ice-binding surface, thereby affecting ice nucleation activity. In conclusion, both repeat number and oligomerization contribute in a seemingly independent manner to the nucleation mechanism of INpros.

KW - precipitation

KW - bioaerosols

KW - PSEUDOMONAS-SYRINGAE

KW - BACTERIA

KW - PRECIPITATION

KW - NUCLEI

KW - PLANTS

KW - IMPACT

KW - MODEL

U2 - 10.1002/2017JD027307

DO - 10.1002/2017JD027307

M3 - Journal article

VL - 123

SP - 1802

EP - 1810

JO - Journal of Geophysical Research

JF - Journal of Geophysical Research

SN - 0148-0227

IS - 3

ER -