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Your search keyword '"Thomson, Andrew"' showing total 24 results
Start Over Author "Thomson, Andrew" Journal journal of biological chemistry
24 results on '"Thomson, Andrew"'

3. NsrR from Streptomyces coelicolor Is a Nitric Oxide-sensing [4Fe-4S] Cluster Protein with a Specialized Regulatory Function

Author

Crack, Jason C., primary, Munnoch, John, additional, Dodd, Erin L., additional, Knowles, Felicity, additional, Al Bassam, Mahmoud M., additional, Kamali, Saeed, additional, Holland, Ashley A., additional, Cramer, Stephen P., additional, Hamilton, Chris J., additional, Johnson, Michael K., additional, Thomson, Andrew J., additional, Hutchings, Matthew I., additional, and Le Brun, Nick E., additional

Published
2015
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14. Novel Binding of HuR and Poly(C)-binding Protein to a Conserved UC-rich Motif within the 3′-Untranslated Region of the Androgen Receptor Messenger RNA

Author

Yeap, Bu B., primary, Voon, Dominic C., additional, Vivian, Julian P., additional, McCulloch, Ross K., additional, Thomson, Andrew M., additional, Giles, Keith M., additional, Czyzyk-Krzeska, Maria F., additional, Furneaux, Henry, additional, Wilce, Matthew C.J., additional, Wilce, Jackie A., additional, and Leedman, Peter J., additional

Published
2002
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15. Spectral Properties of Bacterial Nitric-oxide Reductase

Author

Field, Sarah J., primary, Prior, Louise, additional, Roldán, M. Dolores, additional, Cheesman, Myles R., additional, Thomson, Andrew J., additional, Spiro, Stephen, additional, Butt, Julea N., additional, Watmough, Nicholas J., additional, and Richardson, David J., additional

Published
2002
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22. Three Pseudomonas putida FNR Family Proteins with Different Sensitivities to O2.

Author

Ibrahim, Susan A., Crack, Jason C., Rolfe, Matthew D., Borrero-de Acuňa, José Manuel, Thomson, Andrew J., Le Brun, Nick E., Schobert, Max, Stapleton, Melanie R., and Green, Jeffrey

Subjects
*PSEUDOMONAS putida, *ESCHERICHIA coli, *OXYGEN, *TRANSCRIPTION factors, *BINDING sites
Abstract

The Escherichia coli Fumarate-Nitrate Reduction regulator (FNR) protein is the paradigm for bacterial O2-sensing transcription factors. However, unlike E. coli, some bacterial species possess multiple FNR proteins that presumably have evolved to fulfill distinct roles. Here, three FNR proteins (ANR, PP_3233 and PP_3287) from a single bacterial species, Pseudomonas putida KT2440, have been analyzed. Under anaerobic conditions, all three proteins had spectral properties resembling those of [4Fe-4S] proteins. The reactivity of the ANR [4Fe-4S] cluster with O2 was similar to that of E. coli FNR and during conversion to the apo-protein, via a [2Fe-2S] intermediate, cluster sulfur was retained. Like ANR, reconstituted PP_3233 and PP_3287 were converted to [2Fe-2S] forms when exposed to O2, but their [4Fe-4S] clusters reacted more slowly. Transcription from an FNR-dependent promoter with a consensus FNR-binding site in P. putida and E. coli strains expressing only one FNR protein was consistent with the in vitro responses to O2. Taken together the experimental results suggest that the local environments of the iron-sulfur clusters in the different P. putida FNR proteins influence their reactivity with O2, such that ANR resembles E. coli FNR and is highly-responsive to low concentrations of O2, whereas PP_3233 and PP_3287 have evolved to be less sensitive to O2. [ABSTRACT FROM AUTHOR]

Published
2015
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23. Mechanism of [4Fe-4S](Cys)4 Cluster Nitrosylation Is Conserved among NO-responsive Regulators.

Author

Crack, Jason C., Stapleton, Melanie R., Green, Jeffrey, Thomson, Andrew J., and Le Brun, Nick E.

Subjects
*BISOPROLOL, *NITRATE reductase, *ESCHERICHIA coli, *NITRIC oxide, *GENE expression, *PROTEINS
Abstract

The Fumarate nitrate reduction (FNR) regulator from Escherichia coli controls expression of >300 genes in response to O2 through reaction with its [4Fe-4S] cluster cofactor. FNR is the master switch for the transition between anaerobic and aerobic respiration. In response to physiological concentrations of nitric oxide (NO), FNR also regulates genes, including the nitrate reductase (nar) operon, a major source of endogenous cellular NO, and hmp, which encodes an NO-detoxifying enzyme. Here we show that the [4Fe-4S] cluster of FNR reacts rapidly in a multiphasic reaction with eight NO molecules. Oxidation of cluster sulfide ions (S2-) to sulfane (S0) occurs, some of which remains associated with the protein as Cys persulfide. The nitrosylation products are similar to a pair of dinuclear dinitrosyl iron complexes, [Fe(I)2(NO)4(Cys)2]0, known as Roussin's red ester. A similar reactivity with NO was reported for the Wbl family of [4Fe-4S]-containing proteins found only in actinomycetes, such as Streptomyces and Mycobacteria. These results show that NO reacts via a common mechanism with [4Fe-4S] clusters in phylogenetically unrelated regulatory proteins that, although coordinated by four Cys residues, have different cluster environments. The reactivity of E. coli FNR toward NO, in addition to its sensitivity toward O2, is part of a hierarchal network that monitors, and responds to, NO, both endogenously generated and exogenously derived. [ABSTRACT FROM AUTHOR]

Published
2013
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24. The 3'-Untranslated Region of p21 [Sup wap1] mRNa Is a Composite cis-Acting Sequence Bound By RNA-binding Proteins from Breast Cancer Cells, including HuR and Poly(C)-binding Protein.

Author

Giles, Keith M., Daly, John M., Beveridge, Dianne J., Thomson, Andrew M., Voon, Dominic C., Furneaux, Henry M., Jazayeri, Jalal A., and Leedman, Peter J.

Subjects
*MESSENGER RNA, *RNA-protein interactions, *CANCER cells
Abstract

Reports that the 3'-untranslated region of the cyclin-dependent kinase inhibitor p21[sup WAF1] mRNA is a composite cis-acting sequence bound by RNA-binding proteins from breast cancer cells. Growth inhibition induced by the epidermal growth factor in a variety of cancer cells that overexpress its receptor; Analysis of pertinent topics and relevant issues; Implications on gene structure and regulation.

Published
2003
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