Role of Surface Hydrophobic Residues in the Conformational Stability of Human Lysozyme at Three Different Positions†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (47) ◽  
pp. 14448-14456 ◽  
Author(s):  
Jun Funahashi ◽  
Kazufumi Takano ◽  
Yuriko Yamagata ◽  
Katsuhide Yutani
Keyword(s):  
Conformational Stability ◽  
Human Lysozyme ◽  
Hydrophobic Residues

Role of surface residues in conformational stability of human lysozyme

2000 ◽  
Vol 28 (5) ◽  
pp. A410-A410
Author(s):  
J. Funahashi ◽  
K. Takano ◽  
Y. Yamagata ◽  
M. Nakasako ◽  
K. Yutani
Keyword(s):  
Conformational Stability ◽  
Human Lysozyme

Role of Amino Acid Residues at Turns in the Conformational Stability and Folding of Human Lysozyme†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (29) ◽  
pp. 8655-8665 ◽  
Author(s):  
Kazufumi Takano ◽  
Yuriko Yamagata ◽  
Katsuhide Yutani
Keyword(s):  
Amino Acid ◽  
Conformational Stability ◽  
Amino Acid Residues ◽  
Human Lysozyme

Role of disulfide bonds in folding and secretion of human lysozyme in saccharomycescerevisiae

1988 ◽  
Vol 152 (3) ◽  
pp. 962-967 ◽  
Author(s):  
Yoshio Taniyama ◽  
Yoshio Yamamoto ◽  
Masafumi Nakao ◽  
Masakazu Kikuchi ◽  
Morio Ikehara
Keyword(s):  
Disulfide Bonds ◽  
Human Lysozyme

Role of Cationic Groove and Hydrophobic Residues in Phosphatidylinositol-Dependent Membrane-Binding Properties of Tks5-Phox Homology Domain

2018 ◽  
Vol 3 (4) ◽  
pp. 1205-1214 ◽  
Author(s):  
Sukhamoy Gorai ◽  
Debasish Paul ◽  
Rituparna Borah ◽  
Nandan Haloi ◽  
Manas Kumar Santra ◽  
...  
Keyword(s):  
Membrane Binding ◽  
Binding Properties ◽  
Hydrophobic Residues ◽  
Phox Homology

scholarly journals Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing

2020 ◽  
Vol 117 (7) ◽  
pp. 3543-3550 ◽  
Author(s):  
Yan Huang ◽  
Lu Sun ◽  
Leonidas Pierrakeas ◽  
Linchang Dai ◽  
Lu Pan ◽  
...  
Keyword(s):  
Dna Interaction ◽  
General Strategy ◽  
Histone H2a ◽  
Hydrophobic Residues ◽  
Intrinsically Disordered ◽  
Chromatin Regulators ◽  
A Subunit

The SWR complex edits the histone composition of nucleosomes at promoters to facilitate transcription by replacing the two nucleosomal H2A-H2B (A-B) dimers with H2A.Z-H2B (Z-B) dimers. Swc5, a subunit of SWR, binds to A-B dimers, but its role in the histone replacement reaction was unclear. In this study, we showed that Swc5 uses a tandem DEF/Y motif within an intrinsically disordered region to engage the A-B dimer. A 2.37-Å X-ray crystal structure of the histone binding domain of Swc5 in complex with an A-B dimer showed that consecutive acidic residues and flanking hydrophobic residues of Swc5 form a cap over the histones, excluding histone–DNA interaction. Mutations in Swc5 DEF/Y inhibited the nucleosome editing function of SWR in vitro. Swc5 DEF/Y interacts with histones in vivo, and the extent of this interaction is dependent on the remodeling ATPase of SWR, supporting a model in which Swc5 acts as a wedge to promote A-B dimer eviction. Given that DEF/Y motifs are found in other evolutionary unrelated chromatin regulators, this work provides the molecular basis for a general strategy used repeatedly during eukaryotic evolution to mobilize histones in various genomic functions.

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