scholarly journals Molecular Characterization of the Extracellular Domain of Human Junctional Adhesion Proteins

2021 ◽  
Vol 22 (7) ◽  
pp. 3482
Author(s):  
Christopher Mendoza ◽  
Sai Harsha Nagidi ◽  
Dario Mizrachi
Keyword(s):  
Tertiary Structure ◽  
Extracellular Domain ◽  
The Other ◽  
Immunoglobulin Superfamily ◽  
Adhesive Properties ◽  
The Family ◽  
Heterotypic Interactions ◽  
Hydrophobic Nature ◽  
And Function

The junction adhesion molecule (JAM) family of proteins play central roles in the tight junction (TJ) structure and function. In contrast to claudins (CLDN) and occludin (OCLN), the other membrane proteins of the TJ, whose structure is that of a 4α-helix bundle, JAMs are members of the immunoglobulin superfamily. The JAM family is composed of four members: A, B, C and 4. The crystal structure of the extracellular domain of JAM-A continues to be used as a template to model the secondary and tertiary structure of the other members of the family. In this article, we have expressed the extracellular domains of JAMs fused with maltose-binding protein (MBP). This strategy enabled the work presented here, since JAM-B, JAM-C and JAM4 are more difficult targets due to their more hydrophobic nature. Our results indicate that each member of the JAM family has a unique tertiary structure in spite of having similar secondary structures. Surface plasmon resonance (SPR) revealed that heterotypic interactions among JAM family members can be greatly favored compared to homotypic interactions. We employ the well characterized epithelial cadherin (E-CAD) as a means to evaluate the adhesive properties of JAMs. We present strong evidence that suggests that homotypic or heterotypic interactions among JAMs are stronger than that of E-CADs.

scholarly journals ScII: an abundant chromosome scaffold protein is a member of a family of putative ATPases with an unusual predicted tertiary structure.

1994 ◽  
Vol 127 (2) ◽  
pp. 303-318 ◽  
Author(s):  
N Saitoh ◽  
I G Goldberg ◽  
E R Wood ◽  
W C Earnshaw
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Chromosome Segregation ◽  
Topoisomerase Ii ◽  
Tertiary Structure ◽  
Coiled Coil ◽  
Scaffold Protein ◽  
The Other ◽  
Mitotic Chromosomes ◽  
Chromosome Scaffold

Here, we describe the cloning and characterization of ScII, the second most abundant protein after topoisomerase II, of the chromosome scaffold fraction to be identified. ScII is structurally related to a protein, Smc1p, previously found to be required for accurate chromosome segregation in Saccharomyces cerevisiae. ScII and the other members of the emerging family of SMC1-like proteins are likely to be novel ATPases, with NTP-binding A and B sites separated by two lengthy regions predicted to form an alpha-helical coiled-coil. Analysis of the ScII B site predicted that ScII might use ATP by a mechanism similar to the bacterial recN DNA repair and recombination enzyme. ScII is a mitosis-specific scaffold protein that colocalizes with topoisomerase II in mitotic chromosomes. However, ScII appears not to be associated with the interphase nuclear matrix. ScII might thus play a role in mitotic processes such as chromosome condensation or sister chromatid disjunction, both of which have been previously shown to involve topoisomerase II.

— Zur Morphologie und Funktion des — Helodiden-Aedoeagus (Col.)1

1972 ◽  
Vol 3 (2) ◽  
pp. 81-119 ◽  
Author(s):  
Tord Nyholm
Keyword(s):  
Distal Part ◽  
Comparative Morphology ◽  
Structure And Function ◽  
The Other ◽  
Gradual Change ◽  
Median Lobe ◽  
Initial Form ◽  
The Family ◽  
Different Types ◽  
And Function

AbstractThe structure and function of the aedeagus were investigated in 9 genera of the family Helodidae, most thoroughly in Helodes and Cyphon. On the basis of this investigation, the different types of tegmen and penis represented within the family are described. The tegmen of the Helodidae, which is either entirely devoid of a sclerotized "basal piece" or possesses only rudiments of such, may be divided into three main types; in addition there are a few quite aberrant cases. The penis (median lobe), more interesting from the standpoint of comparative morphology, is extremely diversified. A separation between two main types could however be maintained: one represented by genus Helodes alone, the other by all remaining genera. The Helodes type is more primitive, though at the same time rather specialized in certain details. The second penis type is still more specialized. Its main characteristic is a separate triangular sclerite (a "trigonium") situated ventrally in the distal part of penis. In certain genera it is cleft medially into a pair of moveable appendages ("prosthemata"). A splitting of the penis apex into two lobes ("parameroids") occurs in most species of Helodes, but also among the majority of remaining genera. The evolution of the penis from a supposed primitive initial form towards the Helodes type on one side and the highly specialized type represented by certain species of Cyphon on the other, is outlined and discussed. The importance of a gradual change of the copulatory method for this evolution is particularly stressed. The morphology of the aedeagus as basis for the systematics of the Helodidae is briefly treated. The investigation was also extended to cover representatives of other families, generally regarded as related to the Helodidae. Most of them possess an aedeagus of a rather primitive trilobed type. Deviating from this pattern are the Dascillidae, with the penis completely cleft into one dorsal and one ventral sclerite, and also the Psephenidae. In this family, the penis is supplied with a separate sclerite, apparently homologous with the "trigonium" of the Helodidae and with a similar evolution.

scholarly journals Identification and Characterization of the OsCR4 Extracellular Domain-Interacting Proteins OsCIP1 and OsCIP2 in Rice

2021 ◽  
Author(s):  
Lin-Lin Yan ◽  
Cui-Xia Pu ◽  
Ying Sun
Keyword(s):  
Extracellular Domain ◽  
Vascular Bundles ◽  
Protein Cleavage ◽  
Phylogenetic Tree Analysis ◽  
Cytoplasmic Vesicles ◽  
The Family ◽  
Vegetative And Reproductive Growth ◽  
Mature Seeds ◽  
Identification And Characterization

Abstract The receptor-like kinase OsCR4 plays an important role in vegetative and reproductive growth in rice; it controls embryo morphogenesis, leaf development, and interlocking of the palea and lemma. To identify proteins capable of interacting with the OsCR4 extracellular domain (OsCR4E), we performed a yeast two-hybrid assay and obtained two candidate proteins, OsCIP1 and OsCIP2. Both proteins are cysteine-rich and harbor an N-terminal signal peptide. Localization studies showed OsCIP1-GFP accumulation at the cell surface and OsCIP2-GFP accumulation in cytoplasmic vesicles. Immunoblotting revealed the presence of full-length and truncated OsCIP1-GFP fusion proteins in tobacco leaves and rice roots, and Q62 was identified as the key site for protein cleavage. OsCIP1 was mainly expressed in vascular bundles and the interlocking tissues of the palea and lemma, while OsCIP2 was mainly expressed in mature seeds. Compared to wild type, oscip1 mutant plants exhibited a short seminal root. A phylogenetic tree analysis showed that the homologs of OsCIP1 we identified all belong to the family Gramineae. Our results suggest that OsCIP1 interacts with the extracellular domain of OsCR4.

scholarly journals Characterization of Six Bacteriophages ofSerratia liquefaciens CP6 Isolated from the Sugar Beet Phytosphere

1999 ◽  
Vol 65 (5) ◽  
pp. 1959-1965 ◽  
Author(s):  
Kevin E. Ashelford ◽  
John C. Fry ◽  
Mark J. Bailey ◽  
Aaron R. Jeffries ◽  
Martin J. Day
Keyword(s):  
Sugar Beet ◽  
Burst Size ◽  
Single Step ◽  
The Other ◽  
Cross Hybridization ◽  
The Family ◽  
Step Growth ◽  
Natural Ecology ◽  
Changes Over Time

ABSTRACT Six phages (ΦCP6-1 to ΦCP6-6) that are commonly found in the phytosphere of sugar beet (Beta vulgaris var. Amethyst) were investigated, and their relative impacts on their host (Serratia liquefaciens CP6) were compared. There were fundamental differences between the two most abundant predators of CP6 (ΦCP6-1 and ΦCP6-4). Like ΦCP6-2 and ΦCP6-5, ΦCP6-1 belonged to the family Siphoviridae, while ΦCP6-4 exhibited the morphology of the family Podoviridae. The other phages were members of the family Myoviridae. DNA-DNA cross-hybridization revealed that ΦCP6-1 and ΦCP6-4 had little common DNA, although all of the other phages exhibited some genetic similarity. Like ΦCP6-2, ΦCP6-3, and ΦCP6-5, ΦCP6-1 was capable of forming a lysogenic association with its host, while ΦCP6-4 and ΦCP6-6 appeared to be entirely virulent. Single-step growth curve experiments revealed that ΦCP6-4 had a much shorter latent period and a smaller burst size than ΦCP6-1. Also, ΦCP6-1 could transduce a number of host chromosomal markers with transfer frequencies of 2.9 × 10−9 to 3.9 × 10−7, whereas ΦCP6-4 could not transduce S. liquefaciens CP6 genes. When viewed in the context of the strikingly different temporal niches of these phages, our data provide an insight into how bacteriophage interactions with their hosts might reflect the natural ecology of bacteriophages. Our data also illustrate how the potential for gene transfer changes over time in an environment that supports several different phages.

scholarly journals Historical Perspective of the G Protein-Coupled Receptor Kinase Family

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 555
Author(s):  
Jeffrey L. Benovic
Keyword(s):  
G Protein ◽  
Historical Perspective ◽  
Heterotrimeric G Proteins ◽  
Receptor Kinase ◽  
G Protein Coupled Receptor ◽  
The Family ◽  
Primary Focus ◽  
And Function ◽  
G Protein Coupled

Agonist activation of G protein-coupled receptors promotes sequential interaction of the receptor with heterotrimeric G proteins, G protein-coupled receptor kinases (GRKs), and arrestins. GRKs play a central role in mediating the switch from G protein to arrestin interaction and thereby control processes such as receptor desensitization and trafficking and arrestin-mediated signaling. In this review, I provide a historical perspective on some of the early studies that identified the family of GRKs with a primary focus on the non-visual GRKs. These studies included identification, purification, and cloning of the β-adrenergic receptor kinase in the mid- to late-1980s and subsequent cloning and characterization of additional members of the GRK family. This helped to lay the groundwork for ensuing work focused on understanding the structure and function of these important enzymes.

scholarly journals Study on characterization of chalcone synthase gene from \(\textit{Pueraria lobata}\) and \(\textit{Pueraria mirifica}\) in Vietnam

2021 ◽  
Vol 43 (3) ◽  
pp. 47-58
Author(s):  
Huynh Thi Thu Hue ◽  
Nguyen Minh Phuong ◽  
Nguyen Xuan Canh
Keyword(s):  
Chalcone Synthase ◽  
Stilbene Synthase ◽  
Pueraria Lobata ◽  
Pueraria Mirifica ◽  
Reading Frame ◽  
Chalcone Synthase Gene ◽  
The Family ◽  
Ancient Times ◽  
And Function

Two species of genus Pueraria ((Pueraria lobata (synonym: Pueraria montana var. lobata) and Pueraria mirifica (synonym: Pueraria candollei var. mirifica)) are traditional plants used in medicine since ancient times. These plants have been used and became commercially crucial indigenous medicinal plants. Currently, both roots and flowers of P. mirifica are used as a dietary supplement and functional food for women because of their rich source of phytoestrogen and nutrition. However, little information of genes on both species of Pueraria genus (P. lobata and P. mirifica) are known in Vietnam. The purpose of this research is to support more understanding about Chalcone synthase (CHS) genes by determining and sequence analyzing an encoding region of CHS genes that were isolated from P. lobata and P. mirifica. The full-length open reading frame (ORF) sequence CHS was identified with 1170 bp which encodes 389 amino acids by Sanger sequencing. The isolated CHS gene of P. lobata has no difference in sequence with CHS reported on GenBank (D10223.1), whereas a difference of 26 nucleotide positions in CHS sequence of P. mirifica compared with the published gene sequence (JQ409456.1) as consequential having  97.78% genetic similarity. The CHS genes sequence of P. lobata and P. mirifica are homologous with 98.4% because of having 19 nucleotide differences. Chalcone-stilbene synthase N-C terminal, PLN03173, CHS-like, BH0617, fabH are some important domains predicting the CHS genes. Especially, the family signature ‘GVLFGFGPGLTI’ motif of CHS gene as a part of the active-site scaffold contributes to decide the product of cyclization reactions performing the stereochemistry of cyclization which was also observed in P. lobata and P. mirifica, but it was not included for all members in Fabaceae family. With in sillico analysis, the P. lobata and P. mirifica CHS sequences have highly conserved regions to maintain their structure and function, so that it needs further studies to clarify these points.

Cloning and functional characterization of a high-affinity Na+/dicarboxylate cotransporter from mouse brain

2001 ◽  
Vol 280 (5) ◽  
pp. C1215-C1223 ◽  
Author(s):  
Ana M. Pajor ◽  
Rama Gangula ◽  
Xiaozhou Yao
Keyword(s):  
Electrical Properties ◽  
Mouse Brain ◽  
Functional Characterization ◽  
The Other ◽  
Acidic Ph ◽  
High Affinity ◽  
The Family ◽  
Electrode Voltage ◽  
Menten Constant

Neurons contain a high-affinity Na+/dicarboxylate cotransporter for absorption of neurotransmitter precursor substrates, such as α-ketoglutarate and malate, which are subsequently metabolized to replenish pools of neurotransmitters, including glutamate. We have isolated the cDNA coding for a high-affinity Na+/dicarboxylate cotransporter from mouse brain, called mNaDC-3. The mRNA coding for mNaDC-3 is found in brain and choroid plexus as well as in kidney and liver. The mNaDC-3 transporter has a broad substrate specificity for dicarboxylates, including succinate, α-ketoglutarate, fumarate, malate, and dimethylsuccinate. The transport of citrate is relatively insensitive to pH, but the transport of succinate is inhibited by acidic pH. The Michaelis-Menten constant for succinate in mNaDC-3 is 140 μM in transport assays and 16 μM at −50 mV in two-electrode voltage clamp assays. Transport is dependent on sodium, although lithium can partially substitute for sodium. In conclusion, mNaDC-3 likely codes for the high-affinity Na+/dicarboxylate cotransporter in brain, and it has some unusual electrical properties compared with the other members of the family.

scholarly journals Lectin PLL3, a Novel Monomeric Member of the Seven-Bladed β-Propeller Lectin Family

Molecules ◽  
2019 ◽  
Vol 24 (24) ◽  
pp. 4540 ◽  
Author(s):  
Lukáš Faltinek ◽  
Eva Fujdiarová ◽  
Filip Melicher ◽  
Josef Houser ◽  
Martina Kašáková ◽  
...  
Keyword(s):  
The Other ◽  
Titration Calorimetry ◽  
Gram Negative Bacteria ◽  
Hemagglutination Assay ◽  
Binding Properties ◽  
X Ray Crystallography ◽  
The Family ◽  
Mutualistic Relationship ◽  
Lectin Family

The Photorhabdus species is a Gram-negative bacteria of the family Morganellaceae that is known for its mutualistic relationship with Heterorhabditis nematodes and pathogenicity toward insects. This study is focused on the characterization of the recombinant lectin PLL3 with an origin in P. laumondii subsp. laumondii. PLL3 belongs to the PLL family of lectins with a seven-bladed β-propeller fold. The binding properties of PLL3 were tested by hemagglutination assay, glycan array, isothermal titration calorimetry, and surface plasmon resonance, and its structure was determined by X-ray crystallography. Obtained data revealed that PLL3 binds similar carbohydrates to those that the other PLL family members bind, with some differences in the binding properties. PLL3 exhibited the highest affinity toward l-fucose and its derivatives but was also able to interact with O-methylated glycans and other ligands. Unlike the other members of this family, PLL3 was discovered to be a monomer, which might correspond to a weaker avidity effect compared to homologous lectins. Based on the similarity to the related lectins and their proposed biological function, PLL3 might accompany them during the interaction of P. laumondii with both the nematode partner and the insect host.

Notch1 and Notch3 coordinate for pericyte-induced stabilization of vasculature

2021 ◽  
Author(s):  
Juliann B. Tefft ◽  
Jennifer L. Bays ◽  
Alex Lammers ◽  
Sudong Kim ◽  
Jeroen Eyckmans ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Adherens Junctions ◽  
Notch Pathway ◽  
The Other ◽  
Other Hand ◽  
Endothelial Junctions ◽  
Heterotypic Interactions ◽  
And Function

The Notch pathway regulates complex patterning events in many species and is critical for the proper formation and function of the vasculature. Despite this importance, how the various components of the Notch pathway work in concert is still not well understood. For example, NOTCH1 stabilizes homotypic endothelial junctions, but the role of NOTCH1 in heterotypic interactions is not entirely clear. NOTCH3, on the other hand, is essential for heterotypic interactions of pericytes with the endothelium, but how NOTCH3 signaling in pericytes impacts the endothelium remains elusive. Here, we use in vitro vascular models to investigate whether pericyte-induced stabilization of the vasculature requires cooperation of NOTCH1 and NOTCH3. We observe that both pericyte NOTCH3 and endothelial NOTCH1 are required for stabilization of the endothelium. Loss of either NOTCH3 or NOTCH1 decreases accumulation of VE-cadherin at endothelial adherens junctions and increases the frequency of wider, more motile junctions. We found that DLL4 was the key ligand for simulating NOTCH1 activation in endothelial cells and observed that DLL4 expression in pericytes is dependent on NOTCH3. Altogether, these data suggest that an interplay between pericyte NOTCH3 and endothelial NOTCH1 is critical for pericyte-induced vascular stabilization.

scholarly journals Characterization of Five Transmembrane Proteins: With Focus on the Tweety, Sideroflexin, and YIP1 Domain Families

2021 ◽  
Vol 9 ◽  
Author(s):  
Misty M. Attwood ◽  
Helgi B. Schiöth
Keyword(s):  
Protein Trafficking ◽  
Tertiary Structure ◽  
Transmembrane Proteins ◽  
Functional Roles ◽  
Functional Activities ◽  
Cell Components ◽  
Cell Processes ◽  
And Function ◽  
Tumor Types

Transmembrane proteins are involved in many essential cell processes such as signal transduction, transport, and protein trafficking, and hence many are implicated in different disease pathways. Further, as the structure and function of proteins are correlated, investigating a group of proteins with the same tertiary structure, i.e., the same number of transmembrane regions, may give understanding about their functional roles and potential as therapeutic targets. This analysis investigates the previously unstudied group of proteins with five transmembrane-spanning regions (5TM). More than half of the 58 proteins identified with the 5TM architecture belong to 12 families with two or more members. Interestingly, more than half the proteins in the dataset function in localization activities through movement or tethering of cell components and more than one-third are involved in transport activities, particularly in the mitochondria. Surprisingly, no receptor activity was identified within this dataset in large contrast with other TM groups. The three major 5TM families, which comprise nearly 30% of the dataset, include the tweety family, the sideroflexin family and the Yip1 domain (YIPF) family. We also analyzed the evolutionary origin of these three families. The YIPF family appears to be the most ancient with presence in bacteria and archaea, while the tweety and sideroflexin families are first found in eukaryotes. We found no evidence of common decent for these three families. About 30% of the 5TM proteins have prominent expression in the brain, liver, or testis. Importantly, 60% of these proteins are identified as cancer prognostic markers, where they are associated with clinical outcomes of various tumor types. Nearly 10% of the 5TMs are still not fully characterized and further investigation of their functional activities and expression is warranted. This study provides the first comprehensive analysis of proteins with the 5TM architecture, providing details of their unique characteristics.

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