Recessiveness and Dominance in Barley Mutants Deficient in Mg-Chelatase Subunit D, an AAA Protein Involved in Chlorophyll Biosynthesis.

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Fältnamn	Indikatorer	Metadata
000		04975naa a2200397 4500
001		oai:lup.lub.lu.se:9d7676fb-2a39-43ca-8212-24677cc8ab81
003		SwePub
008		160401s2006 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://lup.lub.lu.se/record/1640922 URI
024	7	a https://doi.org/10.1105/tpc.106.0423742 DOI
040		a (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a art2 swepub-publicationtype
072	7	a ref2 swepub-contenttype
100	1	a Axelsson, Evau Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biok-ea8
245	1 0	a Recessiveness and Dominance in Barley Mutants Deficient in Mg-Chelatase Subunit D, an AAA Protein Involved in Chlorophyll Biosynthesis.
264		c 2006-12-08
264	1	b Oxford University Press (OUP),c 2006
520		a Mg-chelatase catalyzes the insertion of Mg2+ into protoporphyrin IX at the first committed step of the chlorophyll biosynthetic pathway. It consists of three subunits: I, D, and H. The I subunit belongs to the AAA protein superfamily ( ATPases associated with various cellular activities) that is known to form hexameric ring structures in an ATP-dependant fashion. Dominant mutations in the I subunit revealed that it functions in a cooperative manner. We demonstrated that the D subunit forms ATP-independent oligomeric structures and should also be classified as an AAA protein. Furthermore, we addressed the question of cooperativity of the D subunit with barley (Hordeum vulgare) mutant analyses. The recessive behavior in vivo was explained by the absence of mutant proteins in the barley cell. Analogous mutations in Rhodobacter capsulatus and the resulting D proteins were studied in vitro. Mixtures of wild-type and mutant R. capsulatus D subunits showed a lower activity compared with wild-type subunits alone. Thus, the mutant D subunits displayed dominant behavior in vitro, revealing cooperativity between the D subunits in the oligomeric state. We propose a model where the D oligomer forms a platform for the stepwise assembly of the I subunits. The cooperative behavior suggests that the D oligomer takes an active part in the conformational dynamics between the subunits of the enzyme.
650	7	a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng
700	1	a Lundqvist, Joakimu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)mbfy-jlu
700	1	a Sawicki, Artur4 aut
700	1	a Nilsson, Sarau Lund University,Lunds universitet,Proteinkemi, Malmö,Forskargrupper vid Lunds universitet,Protein Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-sni
700	1	a Schröder, Ingridu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biok-isc
700	1	a Al-Karadaghi, Salamu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)mbfys-sa
700	1	a Willows, Robert D4 aut
700	1	a Hansson, Matsu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biok-mha
710	2	a Biokemi och Strukturbiologib Centrum för Molekylär Proteinvetenskap4 org
773	0	t Plant Celld : Oxford University Press (OUP)g 18:12, s. 3606-3616q 18:12<3606-3616x 1040-4651x 1532-298X
856	4	u http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17158606&dopt=Abstracty FULLTEXT
856	4	u http://dx.doi.org/10.1105/tpc.106.042374y FULLTEXT
856	4	u http://www.plantcell.org/content/18/12/3606.full.pdf
856	4 8	u https://lup.lub.lu.se/record/164092
856	4 8	u https://doi.org/10.1105/tpc.106.042374

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Av författaren/redakt...: Axelsson, Eva; Lundqvist, Joaki ...; Sawicki, Artur; Nilsson, Sara; Schröder, Ingrid; Al-Karadaghi, Sa ...; visa fler...; Willows, Robert ...; Hansson, Mats; visa färre...

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