Identification and functional characterization of Histone‐like DNA‐binding protein inNocardia seriolae(NsHLP) involved in cell apoptosis

2019 ◽  
Vol 42 (5) ◽  
pp. 657-666 ◽  
Author(s):  
Wenji Wang ◽  
Jianlin Chen ◽  
Baoshan Liao ◽  
Liqun Xia ◽  
Suying Hou ◽  
...  
Keyword(s):  
Dna Binding ◽  
Cell Apoptosis ◽  
Binding Protein ◽  
Functional Characterization ◽  
Dna Binding Protein

scholarly journals Identification and functional characterization of BTas transactivator as a DNA-binding protein

Virology ◽  
2010 ◽  
Vol 405 (2) ◽  
pp. 408-413 ◽  
Author(s):  
Juan Tan ◽  
Peng Hao ◽  
Rui Jia ◽  
Wei Yang ◽  
Ruichang Liu ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Functional Characterization ◽  
Dna Binding Protein

scholarly journals Characterization of the maize Mutator transposable element MURA transposase as a DNA-binding protein.

1997 ◽  
Vol 17 (9) ◽  
pp. 5165-5175 ◽  
Author(s):  
M I Benito ◽  
V Walbot
Keyword(s):  
Dna Binding ◽  
Transposable Element ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Functional Characterization ◽  
Dna Binding Protein ◽  
Amino Acid Sequence Similarity ◽  
Mobility Shift ◽  
Gel Mobility Shift

The autonomous MuDR element of the Mutator (Mu) transposable element family of maize encodes at least two proteins, MURA and MURB. Based on amino acid sequence similarity, previous studies have reported that MURA is likely to be a transposase. The functional characterization of MURA has been hindered by the instability of its cDNA, mudrA, in Escherichia coli. In this study, we report the first successful stabilization and expression of MURA in Saccharomyces cerevisiae. Gel mobility shift assays demonstrate that MURA is a DNA-binding protein that specifically binds to sequences within the highly conserved Mu element terminal inverted repeats (TIRs). DNase I and 1,10-phenanthroline-copper footprinting of MURA-Mu1 TIR complexes indicate that MURA binds to a conserved approximately 32-bp region in the TIR of Mu1. In addition, MURA can bind to the same region in the TIRs of all tested actively transposing Mu elements but binds poorly to the diverged Mu TIRs of inactive elements. Previous studies have reported a correlation between Mu transposon inactivation and methylation of the Mu element TIRs. Gel mobility shift assays demonstrate that MURA can interact differentially with unmethylated, hemimethylated, and homomethylated TIR substrates. The significance of MURA's interaction with the TIRs of Mu elements is discussed in the context of what is known about the regulation and mechanisms of Mutator activities in maize.

scholarly journals Purification and Characterization of the Coliphage N4-coded Single-stranded DNA Binding Protein

1989 ◽  
Vol 264 (21) ◽  
pp. 12700-12708
Author(s):  
G Lindberg ◽  
S C Kowalczykowski ◽  
J K Rist ◽  
A Sugino ◽  
L B Rothman-Denes
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Purification And Characterization ◽  
Single Stranded Dna
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