Plant chromosomal high mobility group (HMG) proteins

Grasser, Klaus D.

doi:10.1046/j.1365-313x.1995.7020185.x

Cited by 78 publications

(52 citation statements)

References 16 publications

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“…These motifs were originally associated with the high mobility group I (HMG-I) of nuclear proteins and seem to interact with the minor groove of AT-rich regions of nuclear DNA (Grasser 1995). In addition to the two or five AT-hooks of PD1 and PD3, respectively, PD3 possesses eight CxxC motifs, which are presumed to be metal binding sites of the protein (Sato et al 1995).…”

Section: Pd1 and Pd3mentioning

confidence: 99%

New insights into plastid nucleoid structure and functionality

Krupinska¹,

Melonek²,

Krause

2012

Planta

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Investigations over many decades have revealed that nucleoids of higher plant plastids are highly dynamic with regard to their number, their structural organization and protein composition. Membrane attachment and environmental cues seem to determine the activity and functionality of the nucleoids and point to a highly regulated structure-function relationship. The heterogeneous composition and the many functions that are seemingly associated with the plastid nucleoids could be related to the high number of chromosomes per plastid. Recent proteomic studies have brought novel nucleoidassociated proteins into the spotlight and indicated that plastid nucleoids are an evolutionary hybrid possessing prokaryotic nucleoid features and eukaryotic (nuclear) chromatin components, several of which are dually targeted to the nucleus and chloroplasts. Future studies need to unravel if and how plastid-nucleus communication depends on nucleoid structure and plastid gene expression.

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Section: Pd1 and Pd3mentioning

confidence: 99%

New insights into plastid nucleoid structure and functionality

Krupinska¹,

Melonek²,

Krause

2012

Planta

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“…Moreover, proteins with some extent of similarity to HMGI have been found in plants (for review see Ref. 4), bacteria (5), and Drosophila (6).…”

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confidence: 99%

Protein Footprinting Reveals Specific Binding Modes of a High Mobility Group Protein I to DNAs of Different Conformation

Frank¹,

Schwanbeck²,

Wiśniewski

1998

Journal of Biological Chemistry

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The high mobility group proteins I and Y (HMGI/Y) are abundant components of chromatin. They are thought to derepress chromatin, affect the assembly and activity of the transcriptional machinery, and associate with constitutive heterochromatin during mitosis. HMGI/Y protein molecules contain three potential DNA-binding motifs (AT-hooks), but the extent of contacts between DNA and the entire protein has not been determined. We have used a protein-footprinting procedure to map regions of the Chironomus HMGI protein molecule that are involved in contacts with DNA. We find that in the presence of double-stranded DNA all AT-hook motifs are protected against hydroxyl radical proteolysis. In contrast, only two motifs were protected in the presence of four-way junction DNA. Large regions that flank the AT-hook motifs were found to be strongly protected against proteolysis in complexes with interferon-␤ promoter DNA, suggesting amino acid residues outside the AT-hooks considerably contribute to DNA binding.

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“…These were designated as PD1 and PD3 genes and PD1 and PD3 proteins possess AT-hook motifs, originally found in high mobility group I (Y) proteins, and could be shown to interact with the minor groove AT-rich regions of nuclear DNA (Grasser 1995) (Table 1). AT-hook is a small motif, which has a typical sequence pattern of centered glycinearginine-proline (GRP) tri-peptides (Reeves and Nissen 1990).…”

Section: Pd1 and Pd3mentioning

confidence: 99%

Plastidic proteins containing motifs of nuclear transcription factors

Kodama

2007

Plant Biotechnology

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Plant chromosomal high mobility group (HMG) proteins

Cited by 78 publications

References 16 publications

New insights into plastid nucleoid structure and functionality

New insights into plastid nucleoid structure and functionality

Protein Footprinting Reveals Specific Binding Modes of a High Mobility Group Protein I to DNAs of Different Conformation

Plastidic proteins containing motifs of nuclear transcription factors

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