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{{sections|date=June 2018}}
{{sections|date=June 2018}}


In [[botany|plant biology]], [[protease inhibitor (biology)|proteinase inhibitors]] are a family of small [[protein]]s that serve an integral role in the plant’s defense mechanisms against [[Herbivore#Definition_and_related_terms|herbivory]] from [[insect]]s or [[microorganism]]s that may compromise the integrity of the plant. Proteinase inhibitors are present in all plants and are highly concentrated in the storage tissues of the plant as well as portions of the plant that have suffered damage.<ref>{{Cite journal|last=Habib|first=Huma|last2=Fazili|first2=Khalid|date=August 2007|title=Plant protease inhibitors: a defense strategy in plants|url=https://www.academicjournals.org/article/article1380100578_Habeeb%20and%20Khalid.pdf|journal=Biotechnology and Molecular Biology Review|volume=2|issue=3|pages=68-85|via=Academic Journals}}</ref> They work to disrupt the enzymatic ability of the [[digestive enzyme|digestive]] or microbial [[enzymes]] that are present in the [[stomach]] of the attacker resulting in the inability to properly [[digestion|digest]] the plant material. This causes an interference of proper growth and discourages further wounding of the plant by the attacker.<ref>{{Cite journal|last=Fan|first=Shu-Guo|last2=Wu|first2=Guo-Jiang|date=2005|title=Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects|url=https://ejournal.sinica.edu.tw/bbas/content/2005/4/Bot464-01.html|journal=Botanical Bulletin of Academia Sinica|volume=46|pages=273-292|via=}}</ref> Studies have also recently{{when?|date=June 2018}} revealed that some proteinase inhibitors also provide defense for the plant through the possession of [[antimicrobial]] properties providing for the inhibition of [[pathogen]] growth.<ref>{{cite journal | vauthors = Kim JY, Park SC, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y | title = Protease inhibitors from plants with antimicrobial activity | journal = International Journal of Molecular Sciences | volume = 10 | issue = 6 | pages = 2860–72 | date = June 2009 | pmid = 19582234 | pmc = 2705521 | doi = 10.3390/ijms10062860 }}</ref>
In [[botany|plant biology]], [[protease inhibitor (biology)|proteinase inhibitors]] are a family of small [[protein]]s that serve an integral role in the plant’s defense mechanisms against [[Herbivore#Definition and related terms|herbivory]] from [[insect]]s or [[microorganism]]s that may compromise the integrity of the plant. Proteinase inhibitors are present in all plants and are highly concentrated in the storage tissues of the plant as well as portions of the plant that have suffered damage.<ref>{{Cite journal|last=Habib|first=Huma|last2=Fazili|first2=Khalid|date=August 2007|title=Plant protease inhibitors: a defense strategy in plants|url=https://www.academicjournals.org/article/article1380100578_Habeeb%20and%20Khalid.pdf|journal=Biotechnology and Molecular Biology Review|volume=2|issue=3|pages=68–85|via=Academic Journals}}</ref> They work to disrupt the enzymatic ability of the [[digestive enzyme|digestive]] or microbial [[enzymes]] that are present in the [[stomach]] of the attacker resulting in the inability to properly [[digestion|digest]] the plant material. This causes an interference of proper growth and discourages further wounding of the plant by the attacker.<ref>{{Cite journal|last=Fan|first=Shu-Guo|last2=Wu|first2=Guo-Jiang|date=2005|title=Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects|url=https://ejournal.sinica.edu.tw/bbas/content/2005/4/Bot464-01.html|journal=Botanical Bulletin of Academia Sinica|volume=46|pages=273–292|via=}}</ref> Studies have also recently{{when|date=June 2018}} revealed that some proteinase inhibitors also provide defense for the plant through the possession of [[antimicrobial]] properties providing for the inhibition of [[pathogen]] growth.<ref>{{cite journal | vauthors = Kim JY, Park SC, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y | title = Protease inhibitors from plants with antimicrobial activity | journal = International Journal of Molecular Sciences | volume = 10 | issue = 6 | pages = 2860–72 | date = June 2009 | pmid = 19582234 | pmc = 2705521 | doi = 10.3390/ijms10062860 }}</ref>


While proteinase inhibitors are present in plants naturally, production of these proteins for defense is often induced by either wounding of the plant or by chemical signaling through molecules such as [[methyl jasmonate]].<ref name=":0">{{Cite journal|last=Farmer|first=E. E.|last2=Ryan|first2=C. A.|date=1990-10-01|title=Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves.|url=http://www.pnas.org/cgi/doi/10.1073/pnas.87.19.7713|journal=Proceedings of the National Academy of Sciences|volume=87|issue=19|pages=7713–7716|doi=10.1073/pnas.87.19.7713|pmc=54818}}</ref> Both wounding of the plant as well as signaling molecules result in the formation of [[jasmonic acid]], which then induces the [[gene expression]] of proteinase inhibitors. Many other signal cascades as well as the [[Translocation (botany)|translocation]] of signal molecules through the [[phloem]] and [[xylem]] of the plant are also necessary for the production of these inhibitors. Once the proteinase inhibitor has been ingested by the insect, it presents itself as a normal [[Substrate (biology)|substrate]] for the digestive enzymes binding to the active site on the enzyme. This binding of the inhibitor to the proteinase creates a new complex that is very unlikely to dissociate. Once bound, the active site can no longer be accessed by any other substrate and the enzyme can no longer digest the [[amino acid]]s of the plant.<ref>{{Cite journal|last=Lawrence|first=Paulraj|last2=Koundal|first2=Kripa|date=April 15, 2002|title=Plant protease inhibitors in control of phytophagous insects|url=http://www.ejbiotechnology.info/index.php/ejbiotechnology/article/view/v5n1-3/947|journal=Plant Biotechnology|volume=5|issue=1|doi=10.2225/vol5-issue1-fulltext-3|via=Electronic Journal of Biotechnology}}</ref> Without proper digestion, the insect is unable to grow, and may starve if it chooses to remain at the wounded plant. Similar inhibition of growth can be seen in pathogens that interact with these inhibitors.
While proteinase inhibitors are present in plants naturally, production of these proteins for defense is often induced by either wounding of the plant or by chemical signaling through molecules such as [[methyl jasmonate]].<ref name=":0">{{Cite journal|last=Farmer|first=E. E.|last2=Ryan|first2=C. A.|date=1990-10-01|title=Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves.|url=http://www.pnas.org/cgi/doi/10.1073/pnas.87.19.7713|journal=Proceedings of the National Academy of Sciences|volume=87|issue=19|pages=7713–7716|doi=10.1073/pnas.87.19.7713|pmc=54818}}</ref> Both wounding of the plant as well as signaling molecules result in the formation of [[jasmonic acid]], which then induces the [[gene expression]] of proteinase inhibitors. Many other signal cascades as well as the [[Translocation (botany)|translocation]] of signal molecules through the [[phloem]] and [[xylem]] of the plant are also necessary for the production of these inhibitors. Once the proteinase inhibitor has been ingested by the insect, it presents itself as a normal [[Substrate (biology)|substrate]] for the digestive enzymes binding to the active site on the enzyme. This binding of the inhibitor to the proteinase creates a new complex that is very unlikely to dissociate. Once bound, the active site can no longer be accessed by any other substrate and the enzyme can no longer digest the [[amino acid]]s of the plant.<ref>{{Cite journal|last=Lawrence|first=Paulraj|last2=Koundal|first2=Kripa|date=April 15, 2002|title=Plant protease inhibitors in control of phytophagous insects|url=http://www.ejbiotechnology.info/index.php/ejbiotechnology/article/view/v5n1-3/947|journal=Plant Biotechnology|volume=5|issue=1|doi=10.2225/vol5-issue1-fulltext-3|via=Electronic Journal of Biotechnology}}</ref> Without proper digestion, the insect is unable to grow, and may starve if it chooses to remain at the wounded plant. Similar inhibition of growth can be seen in pathogens that interact with these inhibitors.


In order to discover how the production of the inhibitors was induced, scientists exposed [[tomato]] plants to different forms of methyl jasmonate and then [[assay]]ed using [[radial immunodiffusion]] for proteinase inhibitors in leaf juices. A group of tomato plants was sprayed with a solution containing methyl jasmonate, while another group of tomato plants was exposed to methyl jasmonate vapor in air-tight glass chambers. [[Treatment and control groups|Control groups]] were sprayed with a solution or exposed to a vapor that did not contain methyl jasmonate. Both [[Treatment and control groups|experimental groups]] revealed increased proteinase inhibitor production as a result of exposure to [[Volatility (chemistry)|volatile]] methyl jasmonate in comparison to control groups.<ref name=":0" />
In order to discover how the production of the inhibitors was induced, scientists exposed [[tomato]] plants to different forms of methyl jasmonate and then [[assay]]ed using [[radial immunodiffusion]] for proteinase inhibitors in leaf juices. A group of tomato plants was sprayed with a solution containing methyl jasmonate, while another group of tomato plants was exposed to methyl jasmonate vapor in air-tight glass chambers. [[Treatment and control groups|Control groups]] were sprayed with a solution or exposed to a vapor that did not contain methyl jasmonate. Both [[Treatment and control groups|experimental groups]] revealed increased proteinase inhibitor production as a result of exposure to [[Volatility (chemistry)|volatile]] methyl jasmonate in comparison to control groups.<ref name=":0" />

Revision as of 08:33, 27 July 2018

In plant biology, proteinase inhibitors are a family of small proteins that serve an integral role in the plant’s defense mechanisms against herbivory from insects or microorganisms that may compromise the integrity of the plant. Proteinase inhibitors are present in all plants and are highly concentrated in the storage tissues of the plant as well as portions of the plant that have suffered damage.[1] They work to disrupt the enzymatic ability of the digestive or microbial enzymes that are present in the stomach of the attacker resulting in the inability to properly digest the plant material. This causes an interference of proper growth and discourages further wounding of the plant by the attacker.[2] Studies have also recently[when?] revealed that some proteinase inhibitors also provide defense for the plant through the possession of antimicrobial properties providing for the inhibition of pathogen growth.[3]

While proteinase inhibitors are present in plants naturally, production of these proteins for defense is often induced by either wounding of the plant or by chemical signaling through molecules such as methyl jasmonate.[4] Both wounding of the plant as well as signaling molecules result in the formation of jasmonic acid, which then induces the gene expression of proteinase inhibitors. Many other signal cascades as well as the translocation of signal molecules through the phloem and xylem of the plant are also necessary for the production of these inhibitors. Once the proteinase inhibitor has been ingested by the insect, it presents itself as a normal substrate for the digestive enzymes binding to the active site on the enzyme. This binding of the inhibitor to the proteinase creates a new complex that is very unlikely to dissociate. Once bound, the active site can no longer be accessed by any other substrate and the enzyme can no longer digest the amino acids of the plant.[5] Without proper digestion, the insect is unable to grow, and may starve if it chooses to remain at the wounded plant. Similar inhibition of growth can be seen in pathogens that interact with these inhibitors.

In order to discover how the production of the inhibitors was induced, scientists exposed tomato plants to different forms of methyl jasmonate and then assayed using radial immunodiffusion for proteinase inhibitors in leaf juices. A group of tomato plants was sprayed with a solution containing methyl jasmonate, while another group of tomato plants was exposed to methyl jasmonate vapor in air-tight glass chambers. Control groups were sprayed with a solution or exposed to a vapor that did not contain methyl jasmonate. Both experimental groups revealed increased proteinase inhibitor production as a result of exposure to volatile methyl jasmonate in comparison to control groups.[4]

The production of proteinase inhibitors reveals that plants have the ability to alter their defense behavior in response to a threat or direct attack on plant integrity. This complex defense mechanism serves to not only protect the plant from being eaten, but also from pathogen infection requiring both coordination and communication.

References

  1. ^ Habib, Huma; Fazili, Khalid (August 2007). "Plant protease inhibitors: a defense strategy in plants" (PDF). Biotechnology and Molecular Biology Review. 2 (3): 68–85 – via Academic Journals.
  2. ^ Fan, Shu-Guo; Wu, Guo-Jiang (2005). "Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects". Botanical Bulletin of Academia Sinica. 46: 273–292.
  3. ^ Kim JY, Park SC, Hwang I, Cheong H, Nah JW, Hahm KS, Park Y (June 2009). "Protease inhibitors from plants with antimicrobial activity". International Journal of Molecular Sciences. 10 (6): 2860–72. doi:10.3390/ijms10062860. PMC 2705521. PMID 19582234.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  4. ^ a b Farmer, E. E.; Ryan, C. A. (1990-10-01). "Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves". Proceedings of the National Academy of Sciences. 87 (19): 7713–7716. doi:10.1073/pnas.87.19.7713. PMC 54818.
  5. ^ Lawrence, Paulraj; Koundal, Kripa (April 15, 2002). "Plant protease inhibitors in control of phytophagous insects". Plant Biotechnology. 5 (1). doi:10.2225/vol5-issue1-fulltext-3 – via Electronic Journal of Biotechnology.