Role of leucine zipper motif in apoE3 N-terminal domain lipid binding activity

2006 ◽  
Vol 1761 (9) ◽  
pp. 1100-1106 ◽  
Author(s):  
Taichi Yamamoto ◽  
Robert O. Ryan
Keyword(s):  
Leucine Zipper ◽  
Lipid Binding ◽  
Binding Activity ◽  
Leucine Zipper Motif ◽  
Terminal Domain

scholarly journals Interaction of a Swi3 homolog with Sth1 provides evidence for a Swi/Snf-related complex with an essential function in Saccharomyces cerevisiae.

1997 ◽  
Vol 17 (4) ◽  
pp. 1768-1775 ◽  
Author(s):  
I Treich ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Hybrid System ◽  
Transcriptional Activation ◽  
Leucine Zipper ◽  
Leucine Zipper Motif ◽  
Cell Extracts ◽  
Essential Function ◽  
Self Association ◽  
Two Hybrid

The Saccharomyces cerevisiae Swi/Snf complex has a role in remodeling chromatin structure to facilitate transcriptional activation. The complex has 11 components, including Swi1/Adr6, Swi2/Snf2, Swi3, Snf5, Snf6, Snf11, Swp73/Snf12, and Tfg3. Mammalian homologs of these proteins have been shown to form multiple Swi/Snf-related complexes. Here we characterize an S. cerevisiae Swi3 homolog (Swh3) and present evidence that it associates in a complex with a Snf2 homolog, Sthl. We identified Swh3 as a protein that interacts with the N terminus of Snf2 in the two-hybrid system. Swh3 and Swi3 are functionally distinct, and overexpression of one does not compensate for loss of the other. Swh3 is essential for viability and does not activate transcription of reporters. The Snf2 sequence that interacts with Swh3 was mapped to a region conserved in Sth1. We show that Swh3 and Sth1 fusion proteins interact in the two-hybrid system and coimmunoprecipitate from yeast cell extracts. We also map interactions between Swh3 and Sth1 and examine the role of a leucine zipper motif in self-association of Swh3. These findings, together with previous analysis of Sth1, indicate that Swh3 and Sth1 are associated in a complex that is functionally distinct from the Swi/Snf complex and essential for viability.

scholarly journals Replacement of helix 1' enhances the lipid binding activity of apoE3 N-terminal domain

FEBS Journal ◽  
2006 ◽  
Vol 273 (3) ◽  
pp. 558-567 ◽  
Author(s):  
Katherine A. Redmond ◽  
Conrad Murphy ◽  
Vasanthy Narayanaswami ◽  
Robert S. Kiss ◽  
Paul Hauser ◽  
...  
Keyword(s):  
Lipid Binding ◽  
Binding Activity ◽  
Terminal Domain

scholarly journals Glucocorticoid-induced leucine zipper (GILZ)/NF- B interaction: role of GILZ homo-dimerization and C-terminal domain

2006 ◽  
Vol 35 (2) ◽  
pp. 517-528 ◽  
Author(s):  
B. D. Marco ◽  
M. Massetti ◽  
S. Bruscoli ◽  
A. Macchiarulo ◽  
R. D. Virgilio ◽  
...  
Keyword(s):  
Leucine Zipper ◽  
Terminal Domain

scholarly journals Characterization of the Dimerization Domain in BglG, an RNA-Binding Transcriptional Antiterminator fromEscherichia coli

1999 ◽  
Vol 181 (6) ◽  
pp. 1755-1766 ◽  
Author(s):  
Amarelle Boss ◽  
Anat Nussbaum-Shochat ◽  
Orna Amster-Choder
Keyword(s):  
Leucine Zipper ◽  
Rna Binding ◽  
Phosphorylation Site ◽  
Leucine Zipper Motif ◽  
Dimerization Domain ◽  
Specific Sequence ◽  
Carboxy Terminal

ABSTRACT The Escherichia coli transcriptional antiterminator protein BglG inhibits transcription termination of the bgloperon in response to the presence of β-glucosides in the growth medium. BglG is an RNA-binding protein that recognizes a specific sequence partially overlapping the two terminators within thebgl transcript. The activity of BglG is determined by its dimeric state which is modulated by reversible phosphorylation. Thus, only the nonphosphorylated dimer binds to the RNA target site and allows readthrough of transcription. Genetic systems which test dimerization and antitermination in vivo were used to map and delimit the region which mediates BglG dimerization. We show that the last 104 residues of BglG are required for dimerization. Any attempt to shorten this region from the ends or to introduce internal deletions abolished the dimerization capacity of this region. A putative leucine zipper motif is located at the N terminus of this region. The role of the canonical leucines in dimerization was demonstrated by their substitution. Our results also suggest that the carboxy-terminal 70 residues, which follow the leucine zipper, contain another dimerization domain which does not resemble any known dimerization motif. Each of these two regions is necessary but not sufficient for dimerization. The BglG phosphorylation site, His208, resides at the junction of the two putative dimerization domains. Possible mechanisms by which the phosphorylation of BglG controls its dimerization and thus its activity are discussed.

scholarly journals Multiple Links between HD-Zip Proteins and Hormone Networks

2018 ◽  
Vol 19 (12) ◽  
pp. 4047 ◽  
Author(s):  
Giovanna Sessa ◽  
Monica Carabelli ◽  
Marco Possenti ◽  
Giorgio Morelli ◽  
Ida Ruberti
Keyword(s):  
Leucine Zipper ◽  
Developmental Pathways ◽  
Leucine Zipper Motif ◽  
Plant Growth And Development ◽  
Wide Range ◽  
Relevant Role ◽  
Duplication Events ◽  
Environmental Responses ◽  
Zip Genes

HD-Zip proteins are unique to plants, and contain a homeodomain closely linked to a leucine zipper motif, which are involved in dimerization and DNA binding. Based on homology in the HD-Zip domain, gene structure and the presence of additional motifs, HD-Zips are divided into four families, HD-Zip I–IV. Phylogenetic analysis of HD-Zip genes using transcriptomic and genomic datasets from a wide range of plant species indicate that the HD-Zip protein class was already present in green algae. Later, HD-Zips experienced multiple duplication events that promoted neo- and sub-functionalizations. HD-Zip proteins are known to control key developmental and environmental responses, and a growing body of evidence indicates a strict link between members of the HD-Zip II and III families and the auxin machineries. Interactions of HD-Zip proteins with other hormones such as brassinolide and cytokinin have also been described. More recent data indicate that members of different HD-Zip families are directly involved in the regulation of abscisic acid (ABA) homeostasis and signaling. Considering the fundamental role of specific HD-Zip proteins in the control of key developmental pathways and in the cross-talk between auxin and cytokinin, a relevant role of these factors in adjusting plant growth and development to changing environment is emerging.

scholarly journals DNA binding activity of Helicobacter pylori DnaB helicase: the role of the N-terminal domain in modulating DNA binding activities

FEBS Journal ◽  
2011 ◽  
Vol 279 (2) ◽  
pp. 234-250 ◽  
Author(s):  
Ram G. Nitharwal ◽  
Vijay Verma ◽  
Naidu Subbarao ◽  
Santanu Dasgupta ◽  
Nirupam R. Choudhury ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Dna Binding ◽  
Binding Activity ◽  
Terminal Domain ◽  
Dna Binding Activity ◽  
Dnab Helicase

scholarly journals Essential Role of the Conformational Flexibility of Helices 1 and 5 on the Lipid Binding Activity of Apolipophorin-III

2001 ◽  
Vol 276 (36) ◽  
pp. 34162-34166 ◽  
Author(s):  
Jose L. Soulages ◽  
Estela L. Arrese ◽  
Palaniappan S. Chetty ◽  
Veronica Rodriguez
Keyword(s):  
Essential Role ◽  
Conformational Flexibility ◽  
Lipid Binding ◽  
Binding Activity ◽  
Apolipophorin Iii

Analysis of the role of the leucine zipper motif in regulating the ability of AFAP-110 to alter actin filament integrity

2004 ◽  
Vol 91 (3) ◽  
pp. 602-620 ◽  
Author(s):  
Yong Qian ◽  
Amanda S. Gatesman ◽  
Joseph M. Baisden ◽  
Henry G. Zot ◽  
Lidia Cherezova ◽  
...  
Keyword(s):  
Actin Filament ◽  
Leucine Zipper ◽  
Leucine Zipper Motif

scholarly journals Identification of Sperm-Binding Sites in the N-Terminal Domain of Bovine Egg Coat Glycoprotein ZP4

2022 ◽  
Vol 23 (2) ◽  
pp. 762
Author(s):  
Kamila Dilimulati ◽  
Misaki Orita ◽  
Yoshiki Yonahara ◽  
Fabiana Lica Imai ◽  
Naoto Yonezawa
Keyword(s):  
Binding Sites ◽  
Binding Activity ◽  
Binding Region ◽  
Terminal Domain ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Selective Interaction ◽  
Egg Coat

The species-selective interaction between sperm and egg at the beginning of mammalian fertilisation is partly mediated by a transparent envelope called the zona pellucida (ZP). The ZP is composed of three or four glycoproteins (ZP1–ZP4). The functions of the three proteins present in mice (ZP1–ZP3) have been extensively studied. However, the biological role of ZP4, which was found in all other mammals studied so far, has remained largely unknown. Previously, by developing a solid support assay system, we showed that ZP4 exhibits sperm-binding activity in bovines and the N-terminal domain of bovine ZP4 (bZP4 ZP-N1 domain) is a sperm-binding region. Here, we show that bovine sperm bind to the bZP4 ZP-N1 domain in a species-selective manner and that N-glycosylation is not required for sperm-binding activity. Moreover, we identified three sites involved in sperm binding (site I: from Gln-41 to Pro-46, site II: from Leu-65 to Ser-68 and site III: from Thr-108 to Ile-123) in the bZP4 ZP-N1 domain using chimeric bovine/porcine and bovine/human ZP4 recombinant proteins. These results provide in vitro experimental evidence for the role of the bZP4 ZP-N1 domain in mediating sperm binding to the ZP.

scholarly journals Structural and biochemical analyses of Caulobacter crescentus ParB reveal the role of its N-terminal domain in chromosome segregation

2019 ◽  
Author(s):  
Adam S. B. Jalal ◽  
César L. Pastrana ◽  
Ngat T. Tran ◽  
Clare. E. Stevenson ◽  
David M. Lawson ◽  
...  
Keyword(s):  
Dna Binding ◽  
Chromosome Segregation ◽  
Caulobacter Crescentus ◽  
Bacterial Species ◽  
Binding Activity ◽  
Terminal Domain ◽  
Dna Binding Activity

ABSTRACTThe tripartite ParA-ParB-parS complex ensures faithful chromosome segregation in the majority of bacterial species. ParB nucleates on a centromere-like parS site and spreads to neighboring DNA to form a network of protein-DNA complexes. This nucleoprotein network interacts with ParA to partition the parS locus, hence the chromosome to each daughter cell. Here, we determine the co-crystal structure of a C-terminal domain truncated ParB-parS complex from Caulobacter crescentus, and show that its N-terminal domain adopts alternate conformations. The multiple conformations of the N-terminal domain might facilitate the spreading of ParB on the chromosome. Next, using ChIP-seq we show that ParBs from different bacterial species exhibit variation in their intrinsic capability for spreading, and that the N-terminal domain is a determinant of this variability. Finally, we show that the C-terminal domain of Caulobacter ParB possesses no or weak non-specific DNA-binding activity. Engineered ParB variants with enhanced non-specific DNA-binding activity condense DNA in vitro but do not spread further than wild-type in vivo. Taken all together, our results emphasize the role of the N-terminal domain in ParB spreading and faithful chromosome segregation in Caulobacter crescentus.

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