𝔖 Bobbio Scriptorium
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A signature for the HMG-1 box DNA-binding proteins

✍ Scribed by David Landsman; Michael Bustin


Book ID
102760927
Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
965 KB
Volume
15
Category
Article
ISSN
0265-9247

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✦ Synopsis


A diverse group of DNA-binding regulatory proteins share a common structural domain which is homologous to the sequence of a highly conserved and abundant chromosomal protein, HMG-1. Proteins containing this HMG-1 box regulate various cellular functions involving DNA binding, suggesting that the target DNA sequences share a common structural element. Members of this protein family exhibit a dual DNA-binding specificity: each recognizes a unique sequence as well as a common DNA conformation. The highly conserved HMG-1/-2 proteins may modulate the binding of other HMG-1 box proteins to bent DNA. We examine the structural and functional relationships between the proteins, identify their signature? and describe common features of their target DNA elements.


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Structure of human upstream binding fact
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The fifth HMG-box domain in human upstream binding factor (hUBF) contributes to the synthesis of rRNA by RNA polymerase I (Pol I). The 2.0 A resolution crystal structure of this protein has been solved using the single-wavelength anomalous dispersion method (SAD). The crystal structure and the repor