| | |  | | | | Record from Web of Science® | | | | | | |
| Two-component signal transduction |
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| Author(s): Stock AM, Robinson VL, Goudreau PN |
| Source: ANNUAL REVIEW OF BIOCHEMISTRY Volume: 69 Pages: 183-215 Published: 2000 |
| Times Cited: 821 References: 279 |
| Abstract: Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase and a response regulator protein. The histidine protein kinase, which is regulated by environmental stimuli, autophosphorylates at a histidine residue, creating a high-energy phosphoryl group that is subsequently transferred to an aspartate residue in the response regulator protein. Phosphorylation induces a conformational change in the regulatory domain that results in activation of an associated domain that effects the response. The basic scheme is highly adaptable, and numerous variations have provided optimization within specific signaling systems. The domains of two-component proteins are modular and can be integrated into proteins and pathways in a variety of ways, but the core structures and activities are maintained. Thus detailed analyses of a relatively small number of representative proteins provide a foundation for understanding this large family of signaling proteins. |
| Document Type: Review |
| Language: English |
| Reprint Address: Stock, AM (reprint author), Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA |
Addresses:
1. Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Ctr Adv Biotechnol & Med, Piscataway, NJ 08854 USA
2. Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Piscataway, NJ 08854 USA |
| Publisher: ANNUAL REVIEWS, 4139 EL CAMINO WAY, PO BOX 10139, PALO ALTO, CA 94303-0139 USA |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: 361QZ |
| ISSN: 0066-4154 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |