scholarly journals Effects of Spectator Ligands on the Specific Recognition of Intrastrand Platinum-DNA Cross-links by High Mobility Group Box and TATA-binding Proteins

2001 ◽  
Vol 276 (42) ◽  
pp. 38774-38780 ◽  
Author(s):  
Min Wei ◽  
Seth M. Cohen ◽  
Adam P. Silverman ◽  
Stephen J. Lippard
Keyword(s):  
Binding Proteins ◽  
High Mobility ◽  
High Mobility Group ◽  
Specific Recognition ◽  
Tata Binding Proteins ◽  
Cross Links

scholarly journals High Mobility Group Protein-B1 Interacts with Sterol Regulatory Element-binding Proteins to Enhance Their DNA Binding

2005 ◽  
Vol 280 (30) ◽  
pp. 27523-27532 ◽  
Author(s):  
Yuho Najima ◽  
Naoya Yahagi ◽  
Yoshinori Takeuchi ◽  
Takashi Matsuzaka ◽  
Motohiro Sekiya ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Regulatory Element ◽  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Protein ◽  
Sterol Regulatory Element ◽  
Group Protein

scholarly journals Hepatic Nuclear Factor 3 and High Mobility Group I/Y Proteins Bind the Insulin Response Element of the Insulin-Like Growth Factor-Binding Protein-1 Promoter*

Endocrinology ◽  
1997 ◽  
Vol 138 (10) ◽  
pp. 4291-4300 ◽  
Author(s):  
Susanne V. Allander ◽  
Susan K. Durham ◽  
Ann O. Scheimann ◽  
Richard M. Wasserman ◽  
Adisak Suwanichkul ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hormonal Regulation ◽  
Binding Proteins ◽  
Insulin Response ◽  
High Mobility ◽  
High Mobility Group ◽  
Nuclear Factor ◽  
Response Element ◽  
Factor Binding ◽  
Group I

Abstract The insulin response element (IRE) of the human insulin-like growth factor-binding protein-1 (IGFBP-1) promoter contains a palindrome of the T(A/G)TTT sequence crucial to hormonal regulation of many genes. In initial studies of how this IRE participates in hormonal regulation, the electromobility shift assay was used under a variety of conditions to identify IRE-binding proteins. An exhaustive search identified five proteins that specifically bind this IRE; purified proteins were used to show that all five are related to either the high mobility group I/Y (HMGI/Y) or hepatic nuclear factor 3 (HNF3) protein families. Further studies used purified HNF3 and HMGI proteins to show: 1) each protects the IGFBP-1 IRE from deoxyribonuclease I (DNaseI) digestion; and 2) HNF3 but not HMGI/Y binds to the related phosphoenolpyruvate carboxykinase and Apo CIII IREs. A series of IRE mutants with variable responsiveness to insulin were used to show that the presence of a TGTTT sequence in the mutants did parallel, but HMGI/Y and HNF3 binding to the mutants did not parallel, the ability of the mutants to confer the inhibitory effect of insulin. In contrast, HNF3 binding to these IRE mutants roughly correlates with response of the mutants to glucocorticoids. The way by which HNF3 and/or other as yet unidentified IRE-binding proteins confer insulin inhibition to IGFBP-1 transcription and the role of HMGI/Y in IRE function have yet to be established.

FR-66979 Covalently Cross-Links the Binding Domain of the High-Mobility Group I/Y Proteins to DNA

1998 ◽  
Vol 120 (9) ◽  
pp. 2192-2193 ◽  
Author(s):  
Scott R. Rajski ◽  
Samuel B. Rollins ◽  
Robert M. Williams
Keyword(s):  
High Mobility ◽  
Binding Domain ◽  
High Mobility Group ◽  
Group I ◽  
Cross Links
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