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The domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain

Clancy, Paula; Xu, Yibin; van Heeswijk, Wally C; Vasudevan, Subhash; Ollis, David

Description

Adenylyltransferase is a bifunctional enzyme that controls the enzymatic activity of dodecameric glutamine synthetase in Escherichia coli by reversible adenylylation and deadenylylation. Previous studies showed that the two similar but chemically distinct reactions are carried out by separate domains within adenylyltransferase. The N-terminal domain carries the deadenylylation activity, and the C-terminal domain carries the adenylylation activity [Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis...[Show more]

dc.contributor.authorClancy, Paula
dc.contributor.authorXu, Yibin
dc.contributor.authorvan Heeswijk, Wally C
dc.contributor.authorVasudevan, Subhash
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-07T22:48:07Z
dc.identifier.issn1742-464X
dc.identifier.urihttp://hdl.handle.net/1885/26350
dc.description.abstractAdenylyltransferase is a bifunctional enzyme that controls the enzymatic activity of dodecameric glutamine synthetase in Escherichia coli by reversible adenylylation and deadenylylation. Previous studies showed that the two similar but chemically distinct reactions are carried out by separate domains within adenylyltransferase. The N-terminal domain carries the deadenylylation activity, and the C-terminal domain carries the adenylylation activity [Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL & Vasudevan SG (1997) EMBO J16, 5562-5571]. In this study, we further map the domain junctions of adenylyltransferase on the basis of solubility and enzymatic analysis of truncation constructs, and show for the first time that adenylyltransferase has three domains: the two activity domains and a central, probably regulatory (R), domain connected by interdomain Q-linkers (N-Q1-R-Q2-C). The various constructs, which have the opposing domain and or central domain removed, all retain their activity in the absence of their respective nitrogen status indicator, i.e. PII or PII-UMP. A panel of mAbs to adenylyltransferase was used to demonstrate that the cellular nitrogen status indicators, PII and PII-UMP, probably bind in the central regulatory domain to stimulate the adenylylation and deadenylylation reactions, respectively. In the light of these results, intramolecular signaling within adenylyltransferase is discussed.
dc.publisherBlackwell Publishing Ltd
dc.sourceThe FEBS Journal
dc.subjectKeywords: adenylyltransferase; nitrogen; transferase; unclassified drug; adenylation; article; chemical reaction; enzyme analysis; nonhuman; priority journal; protein domain; regulatory mechanism; signal transduction; solubility; Amino Acid Sequence; Catalytic Doma Adenyltransferase; Intramolecular signaling; Monoclonal antibody; Regulatory domain
dc.titleThe domains carrying the opposing activities in adenylyltransferase are separated by a central regulatory domain
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume274
dc.date.issued2007
local.identifier.absfor039999 - Chemical Sciences not elsewhere classified
local.identifier.ariespublicationu4005981xPUB44
local.type.statusPublished Version
local.contributor.affiliationClancy, Paula, James Cook University
local.contributor.affiliationXu, Yibin, Walter and Eliza Hall Institute of Medical Research
local.contributor.affiliationvan Heeswijk, Wally C, Free University Amsterdam
local.contributor.affiliationVasudevan, Subhash, James Cook University
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue11
local.bibliographicCitation.startpage2865
local.bibliographicCitation.lastpage2877
local.identifier.doi10.1111/j.1742-4658.2007.05820.x
dc.date.updated2015-12-07T11:57:35Z
local.identifier.scopusID2-s2.0-34249075095
CollectionsANU Research Publications

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