Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function

2011 ◽  
Vol 40 (47) ◽  
pp. 12619 ◽  
Author(s):  
Jamie L. Michalek ◽  
Angelique N. Besold ◽  
Sarah L. J. Michel
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Proteins ◽  
Histidine Residues ◽  
And Function

scholarly journals Primate-restricted KRAB zinc finger proteins and target retrotransposons control gene expression in human neurons

2019 ◽  
Author(s):  
Priscilla Turelli ◽  
Christopher Playfoot ◽  
Dephine Grun ◽  
Charlène Raclot ◽  
Julien Pontis ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Embryonic Stem ◽  
Zinc Finger Proteins ◽  
Endogenous Retrovirus ◽  
Adult Brain ◽  
Human Endogenous Retrovirus ◽  
Regulatory Sequences ◽  
Human Neurons ◽  
And Function ◽  
Transcription Networks

AbstractIn the first days of embryogenesis, transposable element-embedded regulatory sequences (TEeRS) are silenced by Kruppel-associated box (KRAB)-zinc finger proteins (KZFPs). Many TEeRS are subsequently coopted in transcription networks, but how KZFPs influence this process is largely unknown. We identify ZNF417 and ZNF587 as primate-specific KZFPs repressing HERVK (human endogenous retrovirus K) and SVA (SINE-VNTR-Alu) integrants in human embryonic stem cells (ESC). Expressed in specific regions of the human developing and adult brain, ZNF417/587 keep controlling TEeRS in ESC-derived neurons and brain organoids, secondarily influencing the differentiation and neurotransmission profile of neurons and preventing the induction of neurotoxic retroviral proteins and an interferon-like response. Thus, evolutionarily recent KZFPs and their TE targets partner up to influence human neuronal differentiation and physiology.One Sentence SummaryYoung transposable elements and their protein controllers team up to regulate the differentiation and function of human neurons.

scholarly journals The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain

1999 ◽  
Vol 19 (12) ◽  
pp. 8526-8535 ◽  
Author(s):  
Amy J. Williams ◽  
Stephen C. Blacklow ◽  
Tucker Collins
Keyword(s):  
Zinc Finger ◽  
Transcriptional Regulators ◽  
Zinc Finger Proteins ◽  
Rich Region ◽  
Amino Terminal ◽  
Self Association ◽  
And Function ◽  
Scan Domain ◽  
Oligomerization Domain

ABSTRACT A number of Cys2His2 zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be α-helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.

scholarly journals Engineering Zinc Finger Proteins using Accessory Binding Modules

2012 ◽  
Vol 102 (3) ◽  
pp. 74a
Author(s):  
Kathryn Trenshaw ◽  
Younghoon Kim ◽  
Nathan Yee ◽  
Peiyi Wang ◽  
Charles Schroeder
Keyword(s):  
Zinc Finger ◽  
Zinc Finger Proteins
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