Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases
GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2013
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| Online Access: | http://hdl.handle.net/1721.1/82109 https://orcid.org/0000-0001-5486-2755 |
| _version_ | 1811071674399850496 |
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| author | Sydor, Andrew M. Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Douglas, Colin D. Zamble, Deborah B. Drennan, Catherine L |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Sydor, Andrew M. Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Douglas, Colin D. Zamble, Deborah B. Drennan, Catherine L |
| author_sort | Sydor, Andrew M. |
| collection | MIT |
| description | GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail the bioinorganic characterization of YjiA, a representative member of COG0523 subgroup 9 and the only COG0523 protein to date with high-resolution structural information. We find that YjiA is capable of binding several types of transition metals with dissociation constants in the low micromolar range and that metal binding affects both the oligomeric structure and GTPase activity of the enzyme. Using a combination of X-ray crystallography and site-directed mutagenesis, we identify, among others, a metal-binding site adjacent to the nucleotide-binding site in the GTPase domain that involves a conserved cysteine and several glutamate residues. Mutations of the coordinating residues decrease the impact of metal, suggesting that metal binding to this site is responsible for modulating the GTPase activity of the protein. These findings point toward a regulatory function for these COG0523 GTPases that is responsive to their metal-bound state. |
| first_indexed | 2024-09-23T08:54:52Z |
| format | Article |
| id | mit-1721.1/82109 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T08:54:52Z |
| publishDate | 2013 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/821092022-09-30T12:06:00Z Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases Sydor, Andrew M. Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Douglas, Colin D. Zamble, Deborah B. Drennan, Catherine L Massachusetts Institute of Technology. Department of Biology Massachusetts Institute of Technology. Department of Chemistry Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Drennan, Catherine L. GTPases are critical molecular switches involved in a wide range of biological functions. Recent phylogenetic and genomic analyses of the large, mostly uncharacterized COG0523 subfamily of GTPases revealed a link between some COG0523 proteins and metal homeostasis pathways. In this report, we detail the bioinorganic characterization of YjiA, a representative member of COG0523 subgroup 9 and the only COG0523 protein to date with high-resolution structural information. We find that YjiA is capable of binding several types of transition metals with dissociation constants in the low micromolar range and that metal binding affects both the oligomeric structure and GTPase activity of the enzyme. Using a combination of X-ray crystallography and site-directed mutagenesis, we identify, among others, a metal-binding site adjacent to the nucleotide-binding site in the GTPase domain that involves a conserved cysteine and several glutamate residues. Mutations of the coordinating residues decrease the impact of metal, suggesting that metal binding to this site is responsible for modulating the GTPase activity of the protein. These findings point toward a regulatory function for these COG0523 GTPases that is responsive to their metal-bound state. National Institutes of Health (U.S.) (Grant GM69857) Massachusetts Institute of Technology (Poitras Predoctoral Fellowship) Rutgers University (Douglass College Science, Technology, Engineering, and Math Summer Research Experience Grant) Howard Hughes Medical Institute (MIT Summer Research Experience in Chemical Biology Grant 52005719) 2013-11-13T17:39:34Z 2013-11-13T17:39:34Z 2013-02 2013-02 Article http://purl.org/eprint/type/JournalArticle 0006-2960 1520-4995 http://hdl.handle.net/1721.1/82109 Sydor, Andrew M., Marco Jost, Katherine S. Ryan, Kaitlyn E. Turo, Colin D. Douglas, Catherine L. Drennan, and Deborah B. Zamble. “Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases.” Biochemistry 52, no. 10 (March 12, 2013): 1788-1801. © 2013 American Chemical Society https://orcid.org/0000-0001-5486-2755 en_US http://dx.doi.org/10.1021/bi301600z Biochemistry Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society (ACS) PMC |
| spellingShingle | Sydor, Andrew M. Jost, Marco Ryan, Katherine S. Turo, Kaitlyn E. Douglas, Colin D. Zamble, Deborah B. Drennan, Catherine L Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title | Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title_full | Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title_fullStr | Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title_full_unstemmed | Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title_short | Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases |
| title_sort | metal binding properties of escherichia coli yjia a member of the metal homeostasis associated cog0523 family of gtpases |
| url | http://hdl.handle.net/1721.1/82109 https://orcid.org/0000-0001-5486-2755 |
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