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Title: Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts

Abstract

High mobility group (HMG) proteins of the HMGA family are chromatin-associated proteins that act as architectural factors in nucleoprotein structures involved in gene transcription. To date, HMGA-type proteins have been studied in various higher plant species, but not in lower plants. We have identified two HMGA-type proteins, HMGA1 and HMGA2, encoded in the genome of the moss model Physcomitrella patens. Compared to higher plant HMGA proteins, the two Physcomitrella proteins display some structural differences. Thus, the moss HMGA proteins have six (rather than four) AT-hook DNA-binding motifs and their N-terminal domain lacks similarity to linker histone H1. HMGA2 is expressed in moss protonema and it localises to the cell nucleus. Typical of HMGA proteins, HMGA2 interacts preferentially with A/T-rich DNA, when compared with G/C-rich DNA. In cotransformation assays in Physcomitrella protoplasts, HMGA2 stimulated reporter gene expression. In summary, our data show that functional HMGA-type proteins occur in Physcomitrella.

Authors:
 [1];  [2];  [1];  [3];  [2];  [3]
  1. Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg (Denmark)
  2. greenovation Biotech GmbH, Boetzinger Str. 29b, D-79111 Freiburg (Germany)
  3. Lehrstuhl fuer Pflanzenbiotechnologie, Institut fuer Biologie II, Albert-Ludwigs-Universitaet Freiburg, Schaenzlestr. 1, D-79104 Freiburg (Germany)
Publication Date:
OSTI Identifier:
21143885
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 374; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2008.07.091; PII: S0006-291X(08)01407-1; Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CARBOXYLIC ACIDS; CELL NUCLEI; CHLORINATED ALIPHATIC HYDROCARBONS; CHROMATIN; DNA; ELECTROPHORESIS; GENES; PLANT CELLS; PROTEINS; TRANSCRIPTION

Citation Formats

Lyngaard, Carina, Stemmer, Christian, Stensballe, Allan, Graf, Manuela, Gorr, Gilbert, Decker, Eva, and Grasser, Klaus D. Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts. United States: N. p., 2008. Web. doi:10.1016/j.bbrc.2008.07.091.
Lyngaard, Carina, Stemmer, Christian, Stensballe, Allan, Graf, Manuela, Gorr, Gilbert, Decker, Eva, & Grasser, Klaus D. Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts. United States. doi:10.1016/j.bbrc.2008.07.091.
Lyngaard, Carina, Stemmer, Christian, Stensballe, Allan, Graf, Manuela, Gorr, Gilbert, Decker, Eva, and Grasser, Klaus D. Fri . "Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts". United States. doi:10.1016/j.bbrc.2008.07.091.
@article{osti_21143885,
title = {Physcomitrella HMGA-type proteins display structural differences compared to their higher plant counterparts},
author = {Lyngaard, Carina and Stemmer, Christian and Stensballe, Allan and Graf, Manuela and Gorr, Gilbert and Decker, Eva and Grasser, Klaus D.},
abstractNote = {High mobility group (HMG) proteins of the HMGA family are chromatin-associated proteins that act as architectural factors in nucleoprotein structures involved in gene transcription. To date, HMGA-type proteins have been studied in various higher plant species, but not in lower plants. We have identified two HMGA-type proteins, HMGA1 and HMGA2, encoded in the genome of the moss model Physcomitrella patens. Compared to higher plant HMGA proteins, the two Physcomitrella proteins display some structural differences. Thus, the moss HMGA proteins have six (rather than four) AT-hook DNA-binding motifs and their N-terminal domain lacks similarity to linker histone H1. HMGA2 is expressed in moss protonema and it localises to the cell nucleus. Typical of HMGA proteins, HMGA2 interacts preferentially with A/T-rich DNA, when compared with G/C-rich DNA. In cotransformation assays in Physcomitrella protoplasts, HMGA2 stimulated reporter gene expression. In summary, our data show that functional HMGA-type proteins occur in Physcomitrella.},
doi = {10.1016/j.bbrc.2008.07.091},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 4,
volume = 374,
place = {United States},
year = {2008},
month = {10}
}