Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens

Kiilerich B, Stemmer C, Merkle T, Launholt D, Gorr G, Grasser KD (2008)
Gene 407(1-2): 86-97.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Abstract
High mobility group (HMG) proteins of the HMGB family are chromatin-associated proteins that act as architectural factors in nucleoprotein structures, which regulate DNA-dependent processes including transcription. Members of the HMGB family have been characterised from various mono-and dicot plants, but not from lower plant species. Here, we have identified three candidate HMGB proteins encoded in the genome of the moss Physcomitrella patens. The structurally similar HMGB2 and HMGB3 proteins display the typical overall structure of higher plant HMGB proteins consisting of a central HMG-box DNA-binding domain that is flanked by a basic N-terminal and an acidic C-terminal domain. The HMGB1 protein differs from higher plant HMGB proteins by having a very extensive N-terminal domain and by lacking the acidic C-terminal domain. Like higher plant HMGB proteins, HMGB3 localises to the cell nucleus, but HMGB I is targeted to plastids. Analysis of the HMG-box domains of HMGB1 and HMGB3 by CD revealed that HMGB1box and the HMGB3box have an alpha-helical structure. While the HMGB3box interacts with DNA comparable to typical higher plant counterparts, the HMGB I box has only a low affinity for DNA. Cotransformation assays in Physcomitrella protoplasts demonstrated that expression of HMGB3 resulted in repression of reporter gene expression. In summary, our data show that functional HMGB-type proteins occur in Physcomitrella and most likely in other lower plant species. (c) 2007 Elsevier B.V All rights reserved.
Publishing Year
ISSN
PUB-ID

Cite this

Kiilerich B, Stemmer C, Merkle T, Launholt D, Gorr G, Grasser KD. Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens. Gene. 2008;407(1-2):86-97.
Kiilerich, B., Stemmer, C., Merkle, T., Launholt, D., Gorr, G., & Grasser, K. D. (2008). Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens. Gene, 407(1-2), 86-97.
Kiilerich, B., Stemmer, C., Merkle, T., Launholt, D., Gorr, G., and Grasser, K. D. (2008). Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens. Gene 407, 86-97.
Kiilerich, B., et al., 2008. Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens. Gene, 407(1-2), p 86-97.
B. Kiilerich, et al., “Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens”, Gene, vol. 407, 2008, pp. 86-97.
Kiilerich, B., Stemmer, C., Merkle, T., Launholt, D., Gorr, G., Grasser, K.D.: Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens. Gene. 407, 86-97 (2008).
Kiilerich, Bruno, Stemmer, Christian, Merkle, Thomas, Launholt, Dorte, Gorr, Gilbert, and Grasser, Klaus D. “Chromosomal high mobility group (HMG) proteins of the HMGB-type occurring in the moss Physcomitrella patens”. Gene 407.1-2 (2008): 86-97.
This data publication is cited in the following publications:
This publication cites the following data publications:

3 Citations in Europe PMC

Data provided by Europe PubMed Central.

The dengue vector Aedes aegypti contains a functional high mobility group box 1 (HMGB1) protein with a unique regulatory C-terminus.
Ribeiro FS, de Abreu da Silva IC, Carneiro VC, Belgrano Fdos S, Mohana-Borges R, de Andrade Rosa I, Benchimol M, Souza NR, Mesquita RD, Sorgine MH, Gazos-Lopes F, Vicentino AR, Wu W, de Moraes Maciel R, da Silva-Neto MA, Fantappie MR., PLoS ONE 7(7), 2012
PMID: 22802955
Transcript elongation factor TFIIS is involved in arabidopsis seed dormancy.
Grasser M, Kane CM, Merkle T, Melzer M, Emmersen J, Grasser KD., J. Mol. Biol. 386(3), 2009
PMID: 19150360
Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts.
Lyngaard C, Stemmer C, Stensballe A, Graf M, Gorr G, Decker E, Grasser KD., Biochem. Biophys. Res. Commun. 374(4), 2008
PMID: 18662672

66 References

Data provided by Europe PubMed Central.

The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
Thompson, Nucleic Acids Res. 24(), 1997
A set of plant expression vectors for transcriptional and translational fusions.
Topfer R, Matzeit V, Gronenborn B, Schell J, Steinbiss HH., Nucleic Acids Res. 15(14), 1987
PMID: 3615207
Recognition of distorted DNA structures by HMG domains.
Travers A., Curr. Opin. Struct. Biol. 10(1), 2000
PMID: 10679469
Kinetic analysis of high-mobility-group proteins HMG-1 and HMG-I/Y binding to cholesterol-tagged DNA on a supported lipid monolayer.
Webster CI, Cooper MA, Packman LC, Williams DH, Gray JC., Nucleic Acids Res. 28(7), 2000
PMID: 10710428
HMG-1 enhances HMG-I/Y binding to an A/T-rich enhancer element from the pea plastocyanin gene.
Webster CI, Packman LC, Gray JC., Eur. J. Biochem. 268(11), 2001
PMID: 11389716
High-level expression of secreted complex glycosylated recombinant human erythropoietin in the Physcomitrella Delta-fuc-t Delta-xyl-t mutant.
Weise A, Altmann F, Rodriguez-Franco M, Sjoberg ER, Baumer W, Launhardt H, Kietzmann M, Gorr G., Plant Biotechnol. J. 5(3), 2007
PMID: 17359496
Cloning and characterization of rice HMGB1 gene.
Wu Q, Zhang W, Pwee KH, Kumar PP., Gene 312(), 2003
PMID: 12909345
Rice HMGB1 protein recognizes DNA structures and bends DNA efficiently.
Wu Q, Zhang W, Pwee KH, Kumar PP., Arch. Biochem. Biophys. 411(1), 2003
PMID: 12590928
HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activation.
Zappavigna V, Falciola L, Helmer-Citterich M, Mavilio F, Bianchi ME., EMBO J. 15(18), 1996
PMID: 8890171
Binding to four-way junction DNA: a common property of architectural proteins?
Zlatanova J, van Holde K., FASEB J. 12(6), 1998
PMID: 9535214

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 17980517
PubMed | Europe PMC

Search this title in

Google Scholar