46861
2006
2006
eng
1551
1561
11
113
article
Springer
Berlin
1
--
2006-09-19
--
Segregation distortion in Arabidopsis C24/Col-0 and Col-0/C24 recombinant inbred line populations is due to reduced fertility caused by epistatic interaction of two loci
A new large set of reciprocal recombinant inbred lines (RILs) was created between the Arabidopsis accessions Col-0 and C24 for quantitative trait mapping approaches, consisting of 209 Col-0 x C24 and 214 C24 x Col-0 F-7 RI lines. Genotyping was performed using 110 evenly distributed framework single nucleotide polymorphism markers, yielding a genetic map of 425.70 cM, with an average interval of 3.87 cM. Segregation distortion (SD) was observed in several genomic regions during the construction of the genetic map. Linkage disequilibrium analysis revealed an association between a distorted region at the bottom of chromosome V and a non-distorted region on chromosome IV. A detailed analysis of the RILs for these two regions showed that an SD occurred when homozygous Col-0 alleles on chromosome IV coincided with homozygous C24 alleles at the bottom of chromosome V. Using nearly isogenic lines segregating for the distorted region we confirmed that this genotypic composition leads to reduced fertility and fitness.
Theoretical and applied genetics
10.1007/s00122-006-0402-3
16988816
0040-5752
wos:2006
WOS:000241798000016
Torjek, O (reprint author), Univ Potsdam, Dept Genet, Karl Liebknecht Str 24-25, D-14476 Potsdam, Germany., toerjek@mpimp-golm.mpg.de
importub
2020-05-07T11:50:58+00:00
filename=package.tar
c53a61691c3212b3b6857152fc50c2fe
false
true
Otto Torjek
Hanna Witucka-Wall
Rhonda C. Meyer
Maria von Korff
Barbara Kusterer
Carsten Rautengarten
Thomas Altmann
Geowissenschaften
Institut für Geowissenschaften
Referiert
Import
13445
2005
2005
eng
article
1
--
--
--
Inferring hypotheses on functional relationships of genes : Analysis of the Arabidopsis thaliana subtilase gene family
The gene family of subtilisin-like serine proteases (subtilases) in Arabidopsis thaliana comprises 56 members, divided into six distinct subfamilies. Whereas the members of five subfamilies are similar to pyrolysins, two genes share stronger similarity to animal kexins. Mutant screens confirmed 144 T-DNA insertion lines with knockouts for 55 out of the 56 subtilases. Apart from SDD1, none of the confirmed homozygous mutants revealed any obvious visible phenotypic alteration during growth under standard conditions. Apart from this specific case, forward genetics gave us no hints about the function of the individual 54 non-characterized subtilase genes. Therefore, the main objective of our work was to overcome the shortcomings of the forward genetic approach and to infer alternative experimental approaches by using an integrative biolinformatics and biological approach. Computational analyses based on transcriptional co-expression and co-response pattern revealed at least two expression networks, suggesting that functional redundancy may exist among subtilases with limited similarity. Furthermore, two hubs were identified, which may be involved in signalling or may represent higher-order regulatory factors involved in responses to environmental cues. A particular enrichment of co- regulated genes with metabolic functions was observed for four subtilases possibly representing late responsive elements of environmental stress. The kexin homologs show stronger associations with genes of transcriptional regulation context. Based on the analyses presented here and in accordance with previously characterized subtilases, we propose three main functions of subtilases: involvement in (i) control of development, (ii) protein turnover, and (iii) action as downstream components of signalling cascades
allegro:1991-2014
10102126
Plos computational biology. - 1 (2005), 4, S. 297 - 312
Carsten Rautengarten
Dirk Steinhaeuser
D Bussis
A Stintzi
A Schaller
Joachim Kopka
Thomas Altmann
Institut für Biochemie und Biologie
Referiert
11195
2007
2007
eng
VII, 147 S. : graph. Darst.
doctoralthesis
Potsdam
1
--
--
--
Subtilisin-like serine proteases : in Arabidopsis thaliana (L.) Heynh.
allegro:1991-2014
10103072
Potsdam, Univ., Diss., 2007
Carsten Rautengarten
Institut für Biochemie und Biologie
Nicht referiert