1990
DOI: 10.1073/pnas.87.11.4093
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DNA binding properties of the purified Antennapedia homeodomain.

Abstract: The in vitro DNA binding properties of a purified 68-amino acid Antennapedia homeodomain (Antp HD) peptide have been analyzed. Equilibrium and kinetic binding studies showed that stable DNA-protein complexes are formed with a Kd of 1.6 x 10(-9) M and 1.8 x 10(-10) M, respectively. Heterodimer analysis led to the conclusion that Antp HD interacts in vitro as a monomer with the DNA target sites used in our study. The results of methylation and ethylation interference studies indicated that the Antp HD closely ap… Show more

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Cited by 180 publications
(114 citation statements)
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“…The differences in binding between the specific and non-specific interactions were mainly due to differences in dissociation rates. KD values for the complexes between the Antp homeodomain and the A element have been obtained by equilibrium studies and by kinetic binding studies using the gel shift method, and they have been reported to be 1.6X10 -9 M and 1.8 x 10 -1° M, respectively [10]. These values are even smaller than those obtained in the present study.…”
Section: Association and Dissociation Rates For Specific Binding Of Tcontrasting
confidence: 64%
See 1 more Smart Citation
“…The differences in binding between the specific and non-specific interactions were mainly due to differences in dissociation rates. KD values for the complexes between the Antp homeodomain and the A element have been obtained by equilibrium studies and by kinetic binding studies using the gel shift method, and they have been reported to be 1.6X10 -9 M and 1.8 x 10 -1° M, respectively [10]. These values are even smaller than those obtained in the present study.…”
Section: Association and Dissociation Rates For Specific Binding Of Tcontrasting
confidence: 64%
“…Each homeodomain that is encoded by a homeobox can bind specifically to a region of double-stranded (ds) DNA with a specific recognition sequence [2][3][4][5][6]. The interactions between homeodomains and DNA have been extensively analyzed by foot-printing methods and gel shift assays [6][7][8][9][10][11][12][13][14]. Direct structural analysis of the complexes has also been performed with NMR and X-ray [15][16][17][18][19].…”
Section: Introductionmentioning
confidence: 99%
“…A candidate for the activator protein is CEH-36, a homeodomain protein that is expressed symmetrically in AWC neurons and required for AWC fates (Lanjuin et al 2003;Koga and Ohshima 2004). ceh-36 mutants fail to express both str-2 or srsx-3 in AWC, and CEH-36 and other Otx-class K50 homeodomains bind the sequence TAATCC, which is similar to the AATCCC sequence that activates AWC expression of the srsx-3 promoter (Affolter et al 1990;Schier and Gehring 1993;Lanjuin et al 2003;Chaney et al 2005;Berger et al 2008;Etchberger et al 2009). NSY-7 might compete with CEH-36 or another activator for binding to the compound 11-bp element, specifically repressing expression in AWC ON .…”
Section: Discussionmentioning
confidence: 99%
“…These results emphasize that the DNA binding domain is highly conserved between Bombyx ANTP and Drosophila ANTP (Affolter et al 1990), while the putative domains for transcription activation and/or protein-protein interaction, if any, were altered during Diptera and Lepidoptera evolution. An alternative explanation for this variation could be that the Bombyx ANTP protein expressed in the larval middle silk glands is unique and different from that expressed in Bombyx embryos.…”
Section: Summary Figurementioning
confidence: 75%