Actinomycin D binds strongly and dissociates slowly at the dGpdC site with flanking T/T mismatches

Biochemistry
C Liu, F M Chen

Abstract

Comparative electrophoretic, thermal denaturation, and spectroscopic studies with dodecamers of the form d(ATTA-XGCX-TAAT) and their self-complementary counterparts suggest that actinomycin D (ACTD) binds strongly to a 5'GC3' site with flanking T/T mismatches and moderately to that with C/C mismatches but weakly to those with other G/G or A/A mismatches. The relative binding order is found to be T/T > C/C > G/G > A/A. The ACTD binding affinity for the GC site with T/T mismatches is comparable to the strong binding of self-complementary-XGCY-sequences. Both the ACTD association and dissociation kinetics at the GC site with flanking T/T mismatches require two-exponential fits. The slow component of the association rates is slower than those of the self-complementary sequences, whereas that of the dissociation is only slightly faster than that of the -TGCA- sequence. Interestingly, the slow component of dissociation is decidedly slower than those of -AGCT- and -CGCG- sites and is more than an order of magnitude slower than those with C/C, G/G, and A/A mismatches. These kinetic results are further corroborated by fluorescence measurements using 7-amino-ACTD, a fluorescent analog of ACTD. In addition, fluorescence and absorbance spe...Continue Reading

References

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Citations

Jul 3, 2003·Bioorganic & Medicinal Chemistry·Chia-Hung YangLeung Sheh
May 9, 2003·Nucleic Acids Research·Shan-Ho ChouAndrew H-J Wang
May 16, 2002·Proceedings of the National Academy of Sciences of the United States of America·Shan-Ho ChouFu-Ming Chen
Dec 22, 2015·Cell Reports·Ruth B SiboniJ Andrew Berglund
Nov 1, 1996·Neuron·H A LesterS Mager
Apr 10, 2002·Biochemistry·Fu-Ming Chen, Feng Sha
Aug 26, 1998·Biochemistry·R M WadkinsC S Tung

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