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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1999-5-24
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pubmed:databankReference |
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pubmed:abstractText |
The chromosomal high-mobility-group (HMG) proteins of the HMGI/Y family interact with A/T-rich stretches in duplex DNA, and are considered assistant factors in transcriptional regulation. A cDNA encoding an HMGI/Y protein of 190 amino acid residues was isolated from maize and characterized. Like other plant HMGI/Y proteins, the maize HMGI/Y protein contains four copies of the AT-hook DNA-binding motif and an amino-terminal 'histone H1-like region' with a similarity to the globular domain of H1. The maize hmgi/y gene that was isolated from a genomic DNA library contains a single intron that is localized in the region of sequence similarity to histone H1. Interestingly, the genes encoding plant H1 contain an intron at exactly the same relative position, indicating an evolutionary relationship of the plant genes encoding HMGI/Y and H1 proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
230
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10196467-Amino Acid Sequence,
pubmed-meshheading:10196467-Base Sequence,
pubmed-meshheading:10196467-Cloning, Molecular,
pubmed-meshheading:10196467-Evolution, Molecular,
pubmed-meshheading:10196467-HMGA1a Protein,
pubmed-meshheading:10196467-High Mobility Group Proteins,
pubmed-meshheading:10196467-Histones,
pubmed-meshheading:10196467-Introns,
pubmed-meshheading:10196467-Molecular Sequence Data,
pubmed-meshheading:10196467-Plant Proteins,
pubmed-meshheading:10196467-Restriction Mapping,
pubmed-meshheading:10196467-Sequence Alignment,
pubmed-meshheading:10196467-Transcription Factors,
pubmed-meshheading:10196467-Zea mays
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pubmed:year |
1999
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pubmed:articleTitle |
Plant chromosomal HMGI/Y proteins and histone H1 exhibit a protein domain of common origin.
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pubmed:affiliation |
Institut für Biologie III, Albert-Ludwigs-Universität Freiburg, Schänzlestr. 1, D-79104, Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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