JBC INTERFERin siRNA transfection reagent

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Grasser, KlausD.
Right arrow Articles by Ritt, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grasser, KlausD.
Right arrow Articles by Ritt, C.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 271, Number 51, Issue of December 20, 1996 pp. 32900-32906
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Maize Chromosomal HMGc
TWO CLOSELY RELATED STRUCTURE-SPECIFIC DNA-BINDING PROTEINS SPECIFY A SECOND TYPE OF PLANT HIGH MOBILITY GROUP BOX PROTEIN

(Received for publication, August 8, 1996)

Klaus D. Grasser , Rudi Grimm § and Christoph Ritt

From the Institut für Biologie III, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1, D-79104 Freiburg, and § Hewlett Packard GmbH, Hewlett Packardstrasse 8, D-76337 Waldbronn, Federal Republic of Germany

The chromosomal high mobility group (HMG) proteins are small and abundant non-histone proteins common to eukaryotes. We have purified the maize HMGc protein from immature kernels and characterized it by mass spectrometry and amino acid sequence analysis. HMGc could be resolved into two similar proteins by reversed phase chromatography. Cloning and characterization of the corresponding cDNAs revealed that they encode two closely related maize HMGc proteins, now termed HMGc1 and HMGc2. Their theoretical masses of 15,316 and 15,007 Da are >300 Da lower than the masses determined for the proteins purified from maize, indicating post-translational modifications of the proteins. Despite sequence similarity to maize HMGa (and previously described homologous proteins of other species) amino acid sequence alignments reveal that HMGc is in several conserved regions distinct from these proteins. Consequently, we have identified a novel type of plant protein containing an HMG box DNA binding domain and belonging to the HMG1 protein family. HMGc1 and HMGc2 were expressed in Escherichia coli, purified to homogeneity, and analyzed for their DNA binding properties. They proved to bind to DNA structure-specifically since they formed complexes with DNA minicircles at concentrations ~100-fold lower than the concentrations required to form complexes with linear fragments of identical sequence. Furthermore, HMGc1 and HMGc2 can constrain negative superhelical turns in plasmid DNA.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Plant CellHome page
D. Launholt, T. Merkle, A. Houben, A. Schulz, and K. D. Grasser
Arabidopsis Chromatin-Associated HMGA and HMGB Use Different Nuclear Targeting Signals and Display Highly Dynamic Localization within the Nucleus
PLANT CELL, November 1, 2006; 18(11): 2904 - 2918.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
S. Drea, D. J. Leader, B. C. Arnold, P. Shaw, L. Dolan, and J. H. Doonan
Systematic Spatial Analysis of Gene Expression during Wheat Caryopsis Development
PLANT CELL, August 1, 2005; 17(8): 2172 - 2185.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. M. Krohn, C. Stemmer, P. Fojan, R. Grimm, and K. D. Grasser
Protein Kinase CK2 Phosphorylates the High Mobility Group Domain Protein SSRP1, Inducing the Recognition of UV-damaged DNA
J. Biol. Chem., April 4, 2003; 278(15): 12710 - 12715.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
N. M. Krohn, S. Yanagisawa, and K. D. Grasser
Specificity of the Stimulatory Interaction between Chromosomal HMGB Proteins and the Transcription Factor Dof2 and Its Negative Regulation by Protein Kinase CK2-mediated Phosphorylation
J. Biol. Chem., August 30, 2002; 277(36): 32438 - 32444.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Zhao and G. Grafi
The High Mobility Group I/Y Protein Is Hypophosphorylated in Endoreduplicating Maize Endosperm Cells and Is Involved in Alleviating Histone H1-mediated Transcriptional Repression
J. Biol. Chem., August 25, 2000; 275(35): 27494 - 27499.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Stemmer, A. Schwander, G. Bauw, P. Fojan, and K. D. Grasser
Protein Kinase CK2 Differentially Phosphorylates Maize Chromosomal High Mobility Group B (HMGB) Proteins Modulating Their Stability and DNA Interactions
J. Biol. Chem., January 4, 2002; 277(2): 1092 - 1098.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.