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Volumn 8, Issue 10, 2007, Pages 1110-1114

ds-oligonucleotide-peptide conjugates featuring peptides from the leucine-zipper region of Fos as switchable receptors for the oncoprotein Jun

Author keywords

Conjugation; Fos Jun; Molecular recognition; Oligonucleotides; Peptides; Transcription factors

Indexed keywords

LEUCINE ZIPPER PROTEIN; ONCOPROTEIN; PEPTIDE FRAGMENT; PROTEIN FOS; TRANSCRIPTION FACTOR;

EID: 34547575681     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200700115     Document Type: Article
Times cited : (21)

References (42)
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    • The proto-oncoproteins of the Fos and Jun families are prominent members of the basic-leucine zipper (bZIP) DNA-binding family of proteins: a) Y. Chinenov, T. K. Kerppola, Oncogene 2001, 20, 2438-2452;
    • The proto-oncoproteins of the Fos and Jun families are prominent members of the basic-leucine zipper (bZIP) DNA-binding family of proteins: a) Y. Chinenov, T. K. Kerppola, Oncogene 2001, 20, 2438-2452;
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    • Recombinant proteins containing a 30-amino-acid acidic extension at the N terminus of the Fos leucine zipper have been shown to be efficient inhibitors of AP-1 DNA binding. b M. Olive, D. Krylov, D. R. Echlin, K. Gardner, E. Taparowsky, C. Vinson, J. Biol. Chem. 1997, 272, 18586-18594.
    • Recombinant proteins containing a 30-amino-acid acidic extension at the N terminus of the Fos leucine zipper have been shown to be efficient inhibitors of AP-1 DNA binding. b) M. Olive, D. Krylov, D. R. Echlin, K. Gardner, E. Taparowsky, C. Vinson, J. Biol. Chem. 1997, 272, 18586-18594.
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    • For the synthesis of 3b, two additional equivalents of thiol-oligonucleotide 1 were added portionwise in order to ensure total consumption of peptide 2b, since the HPLC retention times of 2b and 3b are similar.
    • For the synthesis of 3b, two additional equivalents of thiol-oligonucleotide 1 were added portionwise in order to ensure total consumption of peptide 2b, since the HPLC retention times of 2b and 3b are similar.
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    • The synthesis of an oligonucleotide-peptide phosphorothioate conjugate incorporating a peptide with 26 amino acids has been reported: M. Antopolsky, U. Tengvall, S. Auriola, I. Jääskeläinen, S. Rönkkö, P. Honkakoshi, A. Urtti, H. Lönnberg, A. Azhayev, Bioconjugate Chem. 1999, 10, 598-606
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    • The sample of c-Jun used for the assays was obtained by recombinant methods and consists of the following sequence amino acids 262-324, MKAERKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNH
    • The sample of c-Jun used for the assays was obtained by recombinant methods and consists of the following sequence (amino acids 262-324): MKAERKRMRNRIAASKSRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNH.
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    • This dsDNA-peptide derivative was obtained by annealing the oligonucleotide-peptide hybrid 4 with its complementary strand, with 4 being identical to 3b but featuring a different DNA sequence: 5′-GTACGTCTGCATT-3′. This hybrid was prepared by using a similar conjugation protocol to that used in the case of 3a
    • This dsDNA-peptide derivative was obtained by annealing the oligonucleotide-peptide hybrid 4 with its complementary strand, with 4 being identical to 3b but featuring a different DNA sequence: 5′-GTACGTCTGCATT-3′. This hybrid was prepared by using a similar conjugation protocol to that used in the case of 3a.
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    • Although Jun-binding experiments with FOSIz 35aa can not be analyzed by using standard PAGE experiments, the relatively weak interaction of 3b can be considered as a valid control. Preliminary experiments of inhibition of binding of Jun to its consensus DNA sequence confirm that such a truncated peptide is a considerably weaker Jun-trapping agent than our dsDNA-peptide hybrid
    • Although Jun-binding experiments with FOSIz 35aa can not be analyzed by using standard PAGE experiments, the relatively weak interaction of 3b can be considered as a valid control. Preliminary experiments of inhibition of binding of Jun to its consensus DNA sequence confirm that such a truncated peptide is a considerably weaker Jun-trapping agent than our dsDNA-peptide hybrid.
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    • It has been shown that dimeric bZIP proteins can recognize half-site consensus sequences with relative high affinity; this suggests that one of their basic regions can interact with the phosphodiester surface of the DNA in a nonspecific manner: a J. J. Hollenbeck, M. G. Oakley, Bio chemistry 2000, 39, 6380-6389;
    • It has been shown that dimeric bZIP proteins can recognize half-site consensus sequences with relative high affinity; this suggests that one of their basic regions can interact with the phosphodiester surface of the DNA in a nonspecific manner: a) J. J. Hollenbeck, M. G. Oakley, Bio chemistry 2000, 39, 6380-6389;
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    • A method to diagnose single-base-mismatched sequences that relies on the differences in the recognition properties of ss- and ds-DNA has recently been reported: P. C. Ray, Angew. Chem. 2006, 118, 1169-1172;
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.