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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-7-6
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pubmed:abstractText |
The proteins, AlgR3 and AlgP, are involved in the regulation of alginate synthesis in Pseudomonas. They contain multiple repeats of Ala*Ala*Lys*Pro as do several other proteins that resemble histones. The interactions of synthesis oligopeptides composed of repeated Ala*Ala*Lys*Pro or Lys*Lys*Ser*Pro units with DNA were studied by fluorescence of the Fmoc (9-fluorenylmethyloxycarbonyl) group attached to the N-termini of the peptides. DNA quenching of the Fmoc fluorescence of the peptides was used to estimate the apparent association constants for the interaction of Fmoc(AAKP)nOH (n = 2, 4, 8, 18, 32) and of Fmoc (KKSP)nOH (n = 2, 4, 8, 16, 20, 32) with DNA. The Fmoc(AAKP)nOH peptides bind to DNA only at low ionic strength; the Fmoc(KKSP)n OH peptides interact with DNA at both low (0.05 M KCl) and high (0.2 M KCl) salt. At low ionic strength an increase in the number of the repeat units causes an increase in the apparent association constant up to approximately 2 x 10(6) M-1 for both types of peptides at N congruent to 24. The insertion of an AAKTA unit into the middle of the Fmoc(AAKP)8OH peptide increases its affinity to DNA. We propose a model of (AAKP)n and of its interaction with DNA. The repeat unit consists of a single turn of alpha-helix followed by a bend necessitated by Pro. The resultant coiled-coil forms a right-handed superhelix with 10 AAKPs per repeat distance of approximately 33 A.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/algP protein, Pseudomonas aeruginosa
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0269-2139
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
63-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7770455-Amino Acid Sequence,
pubmed-meshheading:7770455-Bacterial Proteins,
pubmed-meshheading:7770455-DNA,
pubmed-meshheading:7770455-DNA-Binding Proteins,
pubmed-meshheading:7770455-Hydrogen Bonding,
pubmed-meshheading:7770455-Models, Molecular,
pubmed-meshheading:7770455-Molecular Sequence Data,
pubmed-meshheading:7770455-Protein Conformation,
pubmed-meshheading:7770455-Protein Structure, Secondary,
pubmed-meshheading:7770455-Pseudomonas aeruginosa,
pubmed-meshheading:7770455-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:7770455-Spectrometry, Fluorescence,
pubmed-meshheading:7770455-Transcription Factors
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pubmed:year |
1995
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pubmed:articleTitle |
Interactions of (Ala*Ala*Lys*Pro)n and (Lys*Lys*Ser*Pro)n with DNA. Proposed coiled-coil structure of AlgR3 and AlgP from Pseudomonas aeruginosa.
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pubmed:affiliation |
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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