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.

ZNF198–FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain

Blood ◽  
2000 ◽  
Vol 96 (2) ◽  
pp. 699-704 ◽  
Author(s):  
Sheng Xiao ◽  
Jennifer G. McCarthy ◽  
Jon C. Aster ◽  
Jonathan A. Fletcher
Keyword(s):  
Tyrosine Kinase ◽  
Growth Factor Receptor ◽  
Chromosomal Translocation ◽  
Rich Region ◽  
Kinase Activation ◽  
Distinctive Type ◽  
Transforming Activity ◽  
Self Association ◽  
Proline Rich Region ◽  
Oligomerization Domain

Abstract An acquired chromosomal translocation, t(8;13)(p11;q11-12), observed in a distinctive type of stem cell leukemia/lymphoma syndrome, leads to the fusion of the 5′ portion of ZNF198 and the 3′ portion of FGFR1. ZNF198–FGFR1 fusion transcripts encode 4 to 10 zinc fingers, a proline-rich region, and the intracellular portion of the FGFR1 (fibroblast growth factor receptor 1) receptor tyrosine kinase. We demonstrate that the ZNF198 proline-rich region constitutes a novel self-association domain. When fused to the intracellular domain of FGFR1, the ZNF198 proline-rich region is sufficient to cause oligomerization, FGFR1 tyrosine kinase activation, and transformation of Ba/F3 cells to IL-3 independent growth.

ZNF198–FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain

Blood ◽  
2000 ◽  
Vol 96 (2) ◽  
pp. 699-704 ◽  
Author(s):  
Sheng Xiao ◽  
Jennifer G. McCarthy ◽  
Jon C. Aster ◽  
Jonathan A. Fletcher
Keyword(s):  
Tyrosine Kinase ◽  
Growth Factor Receptor ◽  
Chromosomal Translocation ◽  
Rich Region ◽  
Kinase Activation ◽  
Distinctive Type ◽  
Transforming Activity ◽  
Self Association ◽  
Proline Rich Region ◽  
Oligomerization Domain

An acquired chromosomal translocation, t(8;13)(p11;q11-12), observed in a distinctive type of stem cell leukemia/lymphoma syndrome, leads to the fusion of the 5′ portion of ZNF198 and the 3′ portion of FGFR1. ZNF198–FGFR1 fusion transcripts encode 4 to 10 zinc fingers, a proline-rich region, and the intracellular portion of the FGFR1 (fibroblast growth factor receptor 1) receptor tyrosine kinase. We demonstrate that the ZNF198 proline-rich region constitutes a novel self-association domain. When fused to the intracellular domain of FGFR1, the ZNF198 proline-rich region is sufficient to cause oligomerization, FGFR1 tyrosine kinase activation, and transformation of Ba/F3 cells to IL-3 independent growth.

scholarly journals Importance of Basic Residues in the Nucleocapsid Sequence for Retrovirus Gag Assembly and Complementation Rescue

1998 ◽  
Vol 72 (11) ◽  
pp. 9034-9044 ◽  
Author(s):  
J. Bradford Bowzard ◽  
Robert P. Bennett ◽  
Neel K. Krishna ◽  
Sandra M. Ernst ◽  
Alan Rein ◽  
...  
Keyword(s):  
Zinc Finger ◽  
Mutational Analysis ◽  
Zinc Fingers ◽  
Leukemia Virus ◽  
Foamy Virus ◽  
Gag Proteins ◽  
Amino Terminal ◽  
C Terminus ◽  
Zinc Finger Motifs ◽  
And Function

ABSTRACT The Gag proteins of Rous sarcoma virus (RSV) and human immunodeficiency virus (HIV) contain small interaction (I) domains within their nucleocapsid (NC) sequences. These overlap the zinc finger motifs and function to provide the proper density to viral particles. There are two zinc fingers and at least two I domains within these Gag proteins. To more thoroughly characterize the important sequence features and properties of I domains, we analyzed Gag proteins that contain one or no zinc finger motifs. Chimeric proteins containing the amino-terminal half of RSV Gag and various portions of the carboxy terminus of murine leukemia virus (MLV) (containing one zinc finger) Gag had only one I domain, whereas similar chimeras with human foamy virus (HFV) (containing no zinc fingers) Gag had at least two. Mutational analysis of the MLV NC sequence and inspection of I domain sequences within the zinc-fingerless C terminus of HFV Gag suggested that clusters of basic residues, but not the zinc finger motif residues themselves, are required for the formation of particles of proper density. In support of this, a simple string of strongly basic residues was found to be able to substitute for the RSV I domains. We also explored the possibility that differences in I domains (e.g., their number) account for differences in the ability of Gag proteins to be rescued into particles when they are unable to bind to membranes. Previously published experiments have shown that such membrane-binding mutants of RSV and HIV (two I domains) can be rescued but that those of MLV (one I domain) cannot. Complementation rescue experiments with RSV-MLV chimeras now map this difference to the NC sequence of MLV. Importantly, the same RSV-MLV chimeras could be rescued by complementation when the block to budding was after, rather than before, transport to the membrane. These results suggest that MLV Gag molecules begin to interact at a much later time after synthesis than those of RSV and HIV.

scholarly journals A Fungal Family of Transcriptional Regulators: the Zinc Cluster Proteins

2006 ◽  
Vol 70 (3) ◽  
pp. 583-604 ◽  
Author(s):  
Sarah MacPherson ◽  
Marc Larochelle ◽  
Bernard Turcotte
Keyword(s):  
Zinc Finger ◽  
Fungal Pathogens ◽  
Budding Yeast ◽  
Transcriptional Regulators ◽  
Zinc Finger Proteins ◽  
Pleiotropic Drug Resistance ◽  
Binding Motifs ◽  
Zinc Cluster ◽  
Primary And Secondary Metabolism ◽  
Wide Range

SUMMARY The trace element zinc is required for proper functioning of a large number of proteins, including various enzymes. However, most zinc-containing proteins are transcription factors capable of binding DNA and are named zinc finger proteins. They form one of the largest families of transcriptional regulators and are categorized into various classes according to zinc-binding motifs. This review focuses on one class of zinc finger proteins called zinc cluster (or binuclear) proteins. Members of this family are exclusively fungal and possess the well-conserved motif CysX2CysX6CysX5-12CysX2CysX6-8Cys. The cysteine residues bind to two zinc atoms, which coordinate folding of the domain involved in DNA recognition. The first- and best-studied zinc cluster protein is Gal4p, a transcriptional activator of genes involved in the catabolism of galactose in the budding yeast Saccharomyces cerevisiae. Since the discovery of Gal4p, many other zinc cluster proteins have been characterized; they function in a wide range of processes, including primary and secondary metabolism and meiosis. Other roles include regulation of genes involved in the stress response as well as pleiotropic drug resistance, as demonstrated in budding yeast and in human fungal pathogens. With the number of characterized zinc cluster proteins growing rapidly, it is becoming more and more apparent that they are important regulators of fungal physiology.

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.

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