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Nickel affects xylem Sap RNase a and converts RNase A to a urease
BACKGROUND: Nickel (Ni) is an essential micronutrient; however, its metabolic or physiological functions in plants and animals are largely uncharacterized. The ribonucleases (RNase, e.g., RNase A) are a large family of hydrolases found in one form or many forms facilitating nitrogen (N) cycling. It...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3878916/ https://www.ncbi.nlm.nih.gov/pubmed/24320827 http://dx.doi.org/10.1186/1471-2229-13-207 |
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author | Bai, Cheng Liu, Liping Wood, Bruce W |
author_facet | Bai, Cheng Liu, Liping Wood, Bruce W |
author_sort | Bai, Cheng |
collection | PubMed |
description | BACKGROUND: Nickel (Ni) is an essential micronutrient; however, its metabolic or physiological functions in plants and animals are largely uncharacterized. The ribonucleases (RNase, e.g., RNase A) are a large family of hydrolases found in one form or many forms facilitating nitrogen (N) cycling. It is currently unknown how either a deficiency or excess of Ni influences the functionality of ribonucleases, like RNase A. This is especially true for perennial crops possessing relatively high Ni requirements. RESULTS: We report that the 'rising’ xylem sap of pecan [Carya illinoinensis (Wangenh.) K. Koch, a long-lived tree] at bud break contains a 14 kDa RNase A (aka, RNase 1), which amount has a 33% greater in Ni-deficient as in Ni-sufficient trees when exposed to Ni ions exhibits ureolytic activity. The homologous 13.4 kDa bovine pancreatic RNase A likewise exhibits ureolytic activity upon exposure to Ni ions. Ni therefore affects enzymatic function of a typically non-metalloenzyme, such as it transforms to an enzyme capable of hydrolyzing a linear amide; thus, converting an endonuclease esterase into a urease. CONCLUSIONS: We conclude that Ni potentially affects the level and activity of RNase A present in the spring xylem sap of pecan trees, and probably in other crops, it has the same influence. The catalytic property of RNase A appears to shift from a nuclease to a urease relying on Ni exposure. This is suggestive that RNase A might possess novel metabolic functionality regarding N-metabolism in perennial plants. The ability of Ni to convert the activity of plant and animal RNase A from that of a ribonuclease to a urease indicates a possible unrecognized beneficial metabolic function of Ni in organisms, while also identifying a potential detrimental effect of excessive Ni on N related metabolic activity if there is sufficient disruption of Ni homeostasis. |
format | Online Article Text |
id | pubmed-3878916 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-38789162014-01-07 Nickel affects xylem Sap RNase a and converts RNase A to a urease Bai, Cheng Liu, Liping Wood, Bruce W BMC Plant Biol Research Article BACKGROUND: Nickel (Ni) is an essential micronutrient; however, its metabolic or physiological functions in plants and animals are largely uncharacterized. The ribonucleases (RNase, e.g., RNase A) are a large family of hydrolases found in one form or many forms facilitating nitrogen (N) cycling. It is currently unknown how either a deficiency or excess of Ni influences the functionality of ribonucleases, like RNase A. This is especially true for perennial crops possessing relatively high Ni requirements. RESULTS: We report that the 'rising’ xylem sap of pecan [Carya illinoinensis (Wangenh.) K. Koch, a long-lived tree] at bud break contains a 14 kDa RNase A (aka, RNase 1), which amount has a 33% greater in Ni-deficient as in Ni-sufficient trees when exposed to Ni ions exhibits ureolytic activity. The homologous 13.4 kDa bovine pancreatic RNase A likewise exhibits ureolytic activity upon exposure to Ni ions. Ni therefore affects enzymatic function of a typically non-metalloenzyme, such as it transforms to an enzyme capable of hydrolyzing a linear amide; thus, converting an endonuclease esterase into a urease. CONCLUSIONS: We conclude that Ni potentially affects the level and activity of RNase A present in the spring xylem sap of pecan trees, and probably in other crops, it has the same influence. The catalytic property of RNase A appears to shift from a nuclease to a urease relying on Ni exposure. This is suggestive that RNase A might possess novel metabolic functionality regarding N-metabolism in perennial plants. The ability of Ni to convert the activity of plant and animal RNase A from that of a ribonuclease to a urease indicates a possible unrecognized beneficial metabolic function of Ni in organisms, while also identifying a potential detrimental effect of excessive Ni on N related metabolic activity if there is sufficient disruption of Ni homeostasis. BioMed Central 2013-12-09 /pmc/articles/PMC3878916/ /pubmed/24320827 http://dx.doi.org/10.1186/1471-2229-13-207 Text en Copyright © 2013 Bai et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Bai, Cheng Liu, Liping Wood, Bruce W Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title | Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title_full | Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title_fullStr | Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title_full_unstemmed | Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title_short | Nickel affects xylem Sap RNase a and converts RNase A to a urease |
title_sort | nickel affects xylem sap rnase a and converts rnase a to a urease |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3878916/ https://www.ncbi.nlm.nih.gov/pubmed/24320827 http://dx.doi.org/10.1186/1471-2229-13-207 |
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