CsoR metalloregulatory protein: function, mechanism and relevance
Transition metals are required constituent in bacterial metabolism to assist in some enzymatic reactions. However, intracellular accumulations of these metal ions are harmful to the bacteria as it can trigger unnecessary redox reactions. To overcome this condition, metalloregulatory proteins assist...
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| Format: | Article |
| Language: | English |
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Universiti Putra Malaysia Press
2017
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| Online Access: | http://psasir.upm.edu.my/id/eprint/58296/ http://psasir.upm.edu.my/id/eprint/58296/1/CsoR%20metalloregulatory%20protein%20function%2C%20mechanism%20and%20relevance.pdf |
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| author | Mangavelu, Ashwaani Mohd Yahaya, Normi Leow, Adam Thean Chor Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha |
| author_facet | Mangavelu, Ashwaani Mohd Yahaya, Normi Leow, Adam Thean Chor Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha |
| author_sort | Mangavelu, Ashwaani |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Transition metals are required constituent in bacterial metabolism to assist in some enzymatic reactions. However, intracellular accumulations of these metal ions are harmful to the bacteria as it can trigger unnecessary redox reactions. To overcome this condition, metalloregulatory proteins assist organisms to adapt to sudden elevated and deprived metal ion concentration in the environment via metal homeostasis. CsoR protein is a copper(I) [Cu(I)] sensing operon repressor that is found to be present in all major classes of eubacteria. This metalloregulatory protein binds to the operator region in its apo state under Cu(I) limiting condition and detaches off from the regulatory region when it binds to the excess cytosolic Cu(I) ion, thus derepressing the expression of genes involved in Cu(I) homeostasis. CsoR proteins exist in dimeric and tetrameric states and form certain coordination geometries upon attachment with Cu(I). Certain CsoR proteins have also been found to possess the ability to bind to other types of metals with various binding affinities in some Gram positive bacteria. The role of this metalloregulatory protein in host pathogen interaction and its relation to bacterial virulence are also discussed. |
| first_indexed | 2025-11-15T10:56:39Z |
| format | Article |
| id | upm-58296 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T10:56:39Z |
| publishDate | 2017 |
| publisher | Universiti Putra Malaysia Press |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-582962018-01-05T07:47:11Z http://psasir.upm.edu.my/id/eprint/58296/ CsoR metalloregulatory protein: function, mechanism and relevance Mangavelu, Ashwaani Mohd Yahaya, Normi Leow, Adam Thean Chor Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha Transition metals are required constituent in bacterial metabolism to assist in some enzymatic reactions. However, intracellular accumulations of these metal ions are harmful to the bacteria as it can trigger unnecessary redox reactions. To overcome this condition, metalloregulatory proteins assist organisms to adapt to sudden elevated and deprived metal ion concentration in the environment via metal homeostasis. CsoR protein is a copper(I) [Cu(I)] sensing operon repressor that is found to be present in all major classes of eubacteria. This metalloregulatory protein binds to the operator region in its apo state under Cu(I) limiting condition and detaches off from the regulatory region when it binds to the excess cytosolic Cu(I) ion, thus derepressing the expression of genes involved in Cu(I) homeostasis. CsoR proteins exist in dimeric and tetrameric states and form certain coordination geometries upon attachment with Cu(I). Certain CsoR proteins have also been found to possess the ability to bind to other types of metals with various binding affinities in some Gram positive bacteria. The role of this metalloregulatory protein in host pathogen interaction and its relation to bacterial virulence are also discussed. Universiti Putra Malaysia Press 2017 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/58296/1/CsoR%20metalloregulatory%20protein%20function%2C%20mechanism%20and%20relevance.pdf Mangavelu, Ashwaani and Mohd Yahaya, Normi and Leow, Adam Thean Chor and Mohamad Ali, Mohd Shukuri and Raja Abdul Rahman, Raja Noor Zaliha (2017) CsoR metalloregulatory protein: function, mechanism and relevance. Pertanika Journal of Scholarly Research Reviews, 3 (1). pp. 24-31. ISSN 2462-2028 http://pjsrr.upm.edu.my/wp-content/uploads/2017/07/PJSRR-2017-31-24-31b.pdf |
| spellingShingle | Mangavelu, Ashwaani Mohd Yahaya, Normi Leow, Adam Thean Chor Mohamad Ali, Mohd Shukuri Raja Abdul Rahman, Raja Noor Zaliha CsoR metalloregulatory protein: function, mechanism and relevance |
| title | CsoR metalloregulatory protein: function, mechanism and relevance |
| title_full | CsoR metalloregulatory protein: function, mechanism and relevance |
| title_fullStr | CsoR metalloregulatory protein: function, mechanism and relevance |
| title_full_unstemmed | CsoR metalloregulatory protein: function, mechanism and relevance |
| title_short | CsoR metalloregulatory protein: function, mechanism and relevance |
| title_sort | csor metalloregulatory protein: function, mechanism and relevance |
| url | http://psasir.upm.edu.my/id/eprint/58296/ http://psasir.upm.edu.my/id/eprint/58296/ http://psasir.upm.edu.my/id/eprint/58296/1/CsoR%20metalloregulatory%20protein%20function%2C%20mechanism%20and%20relevance.pdf |