Exzision einer persistierenden Pupillarmembran

Demeler, U

doi:10.1007/978-3-642-88589-1_221

Cited by 1 publication

(1 citation statement)

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“…Optimization was performed by 2-dimensional spectrum analysis (2DSA) 70 with simultaneous removal of time-and radially-invariant noise contributions 71 . After inspection of the 2DSA solutions, the fits were further refined using the parametrically constrained spectrum analysis (PCSA) 72 , coupled with Monte Carlo analysis to measure confidence limits for the determined parameters 73 . The calculations are computationally intensive and were carried out on high performance computing platforms 74 Email address: karen.glass@acphs.edu Present Addresses †If an author's address is different than the one given in the affiliation line, this information may be included here.…”

Section: Analytical Ultracentrifugationmentioning

confidence: 99%

The BRPF1 bromodomain is a molecular reader of di-acetyllysine

Juliet

Lubula

Cornilescu

et al. 2020

Preprint

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ABSTRACTBromodomain-containing proteins are often part of chromatin-modifying complexes, and their activity can lead to altered expression of genes that drive cancer, inflammation and neurological disorders in humans. Bromodomain-PHD finger protein 1 (BRPF1) is part of the MOZ (monocytic leukemic zinc-finger protein) HAT (histone acetyltransferase) complex, which is associated with chromosomal translocations known to contribute to the development of acute myeloid leukemia (AML). BRPF1 contains a unique combination of chromatin reader domains including two plant homeodomain (PHD) fingers separated by a zinc knuckle (PZP domain), a bromodomain, and a proline-tryptophan-tryptophan-proline (PWWP) domain. BRPF1 is known to recruit the MOZ HAT complex to chromatin by recognizing acetylated lysine residues on the N-terminal histone tail region through its bromodomain. However, histone proteins can contain several acetylation modifications on their N-terminus, and it is unknown how additional marks influence bromodomain recruitment to chromatin. Here, we identify the BRPF1 bromodomain as a selective reader of di-acetyllysine modifications on histone H4. We used ITC assays to characterize the binding of di-acetylated histone ligands to the BRPF1 bromodomain and found that the domain binds preferentially to histone peptides H4K5acK8ac and H4K5acK12ac. Analytical ultracentrifugation (AUC) experiments revealed that the monomeric state of the BRPF1 bromodomain coordinates di-acetylated histone ligands. NMR chemical shift perturbation studies, along with binding and mutational analyses, revealed non-canonical regions of the bromodomain-binding pocket that are important for histone tail recognition. Together, our findings provide critical information on how the combinatorial action of post-translational modifications can modulate BRPF1 bromodomain binding and specificity.

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