Crystal structure of the BAZ2B TAM domain

Feng, Yingying; Chen, Sizhuo; Zhou, Mengqi; Zhang, Jin; Min, Jinrong; Liu, Ke

doi:10.1016/j.heliyon.2022.e09873

Cited by 2 publications

(4 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…EMSA experiments showed that the MBD MeCP2 domain exhibited a preference for methylated DNA, whereas TAM Baz2B and TAM–AT1–AT2 Baz2B did not show such specificity (Figure 2A ). This observation is consistent with recent data showing that TAM Baz2B has similar DNA binding affinity for methylated and unmethylated DNA ( 47 ). We conclude that TAM Baz2A and TAM Baz2B , together with three other mammalian MBD proteins (MBD3, MBD5 and MBD6), do not specifically bind methylated DNA ( 12 , 47 , 73 , 74 ).…”

Section: Resultssupporting

confidence: 93%

“…This observation is consistent with recent data showing that TAM Baz2B has similar DNA binding affinity for methylated and unmethylated DNA ( 47 ). We conclude that TAM Baz2A and TAM Baz2B , together with three other mammalian MBD proteins (MBD3, MBD5 and MBD6), do not specifically bind methylated DNA ( 12 , 47 , 73 , 74 ).…”

Section: Resultssupporting

confidence: 93%

“…Interestingly, only the structure of TAM Baz2A was solved in the presence of DNA, demonstrating binding to the DNA backbone in a sequence-unspecific manner. However, the apostructure of TAM Baz2B was resolved despite the presence of DNA in the experimental setup ( 47 ). Our sequence alignment data ( Supplementary Figure S1A ) indicated the potential presence of nucleic acid binding properties in the C-terminus of the TAM Baz2B , suggesting a similarity to AT-hook motifs (TAM-AT1-AT2 Baz2B ).…”

Section: Resultsmentioning

confidence: 99%

“…Additionally, in the X-ray structure, TAM Baz2B is observed as a dimer ( 47 ). However, as suggested by the authors, this dimeric arrangement may be attributed to crystallization artefacts ( 60 ).…”

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Biochemical and cellular insights into the Baz2B protein, a non-catalytic subunit of the chromatin remodeling complex

Breindl,

Spitzer,

Gerasimaitė

et al. 2023

Nucleic Acids Research

View full text Add to dashboard Cite

Baz2B is a regulatory subunit of the ATP-dependent chromatin remodeling complexes BRF1 and BRF5, which control access to DNA during DNA-templated processes. Baz2B has been implicated in several diseases and also in unhealthy ageing, however limited information is available on the domains and cellular roles of Baz2B. To gain more insight into the Baz2B function, we biochemically characterized the TAM (Tip5/ARBP/MBD) domain with the auxiliary AT-hook motifs and the bromodomain (BRD). We observed alterations in histone code recognition in bromodomains carrying cancer-associated point mutations, suggesting their potential involvement in disease. Furthermore, the depletion of Baz2B in the Hap1 cell line resulted in altered cell morphology, reduced colony formation and perturbed transcriptional profiles. Despite that, super-resolution microscopy images revealed no changes in the overall chromatin structure in the absence of Baz2B. These findings provide insights into the biological function of Baz2B.

show abstract