Unknown

Dataset Information

0

The high mobility group box: the ultimate utility player of a cell.


ABSTRACT: High mobility group (HMG) box proteins are abundant and ubiquitous DNA binding proteins with a remarkable array of functions throughout the cell. The structure of the HMG box DNA binding domain and general mechanisms of DNA binding and bending have been known for more than a decade. However, new mechanisms that regulate HMG box protein intracellular translocation, and by which HMG box proteins recognize DNA with and without sequence specificity, have only recently been uncovered. This review focuses primarily on the Sry-like HMG box family, HMGB1, and mitochondrial transcription factor A. For these proteins, structural and biochemical studies have shown that HMG box protein modularity, interactions with other DNA binding proteins and cellular receptors, and post-translational modifications are key regulators of their diverse functions.

SUBMITTER: Malarkey CS 

PROVIDER: S-EPMC4437563 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

The high mobility group box: the ultimate utility player of a cell.

Malarkey Christopher S CS   Churchill Mair E A ME  

Trends in biochemical sciences 20121113 12


High mobility group (HMG) box proteins are abundant and ubiquitous DNA binding proteins with a remarkable array of functions throughout the cell. The structure of the HMG box DNA binding domain and general mechanisms of DNA binding and bending have been known for more than a decade. However, new mechanisms that regulate HMG box protein intracellular translocation, and by which HMG box proteins recognize DNA with and without sequence specificity, have only recently been uncovered. This review foc  ...[more]

Similar Datasets

| S-EPMC7407638 | biostudies-literature
2023-07-28 | GSE216423 | GEO
| S-EPMC6800136 | biostudies-literature
| S-EPMC1459676 | biostudies-literature
| S-EPMC5886030 | biostudies-literature
2008-11-19 | E-GEOD-12204 | biostudies-arrayexpress
| S-EPMC6678463 | biostudies-literature
| S-EPMC3999251 | biostudies-literature
| S-EPMC3293110 | biostudies-literature
| S-EPMC7036925 | biostudies-literature