Taken together, current evidence suggests a role for Trr1p in iron metabolism, possibly as the elusive eukaryotic intracellular transporter. To characterize the exact mechanism of Trr1p in iron metabolism, the involvement of Trr1p in iron uptake and iron–sulfur cluster formation should be explored.
Acknowledgments
This work was supported by the Korea Research Foundation Grant funded by the Korean Government (MOEHRD, Basic Research Promotion Fund) (KRF-2007-313-C00456).
Keywords
HMG; HMGB; DNA; Kink; Cruciform; Binding; Kinetics; Gel shift
Double-stranded DNA Angiotensin 1/2 (5-7) among the least flexible biopolymers. The local stiffness of DNA is reflected in its persistence length, P, (～150 bp) [1]. The global flexibility of naked DNA in solution is insufficient to allow the degree of compaction required for packaging within cells, or for deformed structures involved in DNA replication, recombination, and transcriptional control. While some controversy exists concerning the accuracy of predictive models for DNA flexibility over short lengths [2], [3] and [4], it is clear that short lengths of DNA require proteins to induce strongly bent and looped conformations.
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