Basic Residue at Position 14 Is Not Required for Fast Assembly and Disassembly Kinetics in Neural Cadherin

Biochemistry ◽  
2015 ◽  
Vol 54 (3) ◽  
pp. 836-843 ◽  
Author(s):  
Nagamani Vunnam ◽  
Nathan I. Hammer ◽  
Susan Pedigo
Keyword(s):  
Basic Residue ◽  
Neural Cadherin

scholarly journals Basic Residue at Position 14 is not Required for Fast Assembly and Disassembly Kinetics in Neural Cadherin

2015 ◽  
Vol 108 (2) ◽  
pp. 51a
Author(s):  
Nagamani Vunnam ◽  
Nathan I. Hammer ◽  
Susan Pedigo
Keyword(s):  
Basic Residue ◽  
Neural Cadherin

scholarly journals Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A

2021 ◽  
Vol 22 (3) ◽  
pp. 1036
Author(s):  
Xuguang Lin ◽  
Kenichi Watanabe ◽  
Masahiro Kuragano ◽  
Kiyotaka Tokuraku
Keyword(s):  
Amino Acid ◽  
Serum Amyloid A ◽  
Animal Species ◽  
Amino Acid Sequences ◽  
Serum Amyloid ◽  
Mouse Serum ◽  
Aa Amyloidosis ◽  
Basic Residue ◽  
Amyloid A ◽  
Serum Amyloid A Protein

Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis.

scholarly journals Basic Residue Clusters in Intrinsically Disordered Regions of Peripheral Membrane Proteins: Modulating 2D Diffusion on Cell Membranes

Physchem ◽  
2021 ◽  
Vol 1 (2) ◽  
pp. 152-162
Author(s):  
Miquel Pons
Keyword(s):  
Membrane Proteins ◽  
Electrostatic Interactions ◽  
Lipid Membrane ◽  
Conformational Ensemble ◽  
Basic Residue ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Peripheral Membrane Proteins ◽  
Charged Residues ◽  
Disordered Regions

A large number of peripheral membrane proteins transiently interact with lipids through a combination of weak interactions. Among them, electrostatic interactions of clusters of positively charged amino acid residues with negatively charged lipids play an important role. Clusters of charged residues are often found in intrinsically disordered protein regions, which are highly abundant in the vicinity of the membrane forming what has been called the disordered boundary of the cell. Beyond contributing to the stability of the lipid-bound state, the pattern of charged residues may encode specific interactions or properties that form the basis of cell signaling. The element of this code may include, among others, the recognition, clustering, and selective release of phosphatidyl inositides, lipid-mediated protein-protein interactions changing the residence time of the peripheral membrane proteins or driving their approximation to integral membrane proteins. Boundary effects include reduction of dimensionality, protein reorientation, biassing of the conformational ensemble of disordered regions or enhanced 2D diffusion in the peri-membrane region enabled by the fuzzy character of the electrostatic interactions with an extended lipid membrane.

Hormonal dependency of neural cadherin in the binding of round spermatids to Sertoli cells in vitro.

Endocrinology ◽  
1996 ◽  
Vol 137 (9) ◽  
pp. 3877-3883 ◽  
Author(s):  
K J Perryman ◽  
P G Stanton ◽  
K L Loveland ◽  
R I McLachlan ◽  
D M Robertson
Keyword(s):  
Sertoli Cells ◽  
Neural Cadherin

scholarly journals Nickel Reduces Calcium-Dependant Dimerization by Neural Cadherin

2015 ◽  
Vol 108 (2) ◽  
pp. 212a ◽  
Author(s):  
Matthew P. Dukes ◽  
Rhianon Kay Rowe ◽  
Susan Pedigo
Keyword(s):  
Neural Cadherin

scholarly journals The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone

2020 ◽  
Vol 48 (16) ◽  
pp. 9273-9284
Author(s):  
Ningning Zhang ◽  
Li Guo ◽  
Li Huang
Keyword(s):  
Elevated Temperatures ◽  
Normal Growth ◽  
Strand Exchange ◽  
Nucleic Acid Binding ◽  
Basic Residue ◽  
Rna Chaperone ◽  
Sulfolobus Islandicus ◽  
Nucleic Acid Binding Proteins ◽  
Rna Unwinding

Abstract Nucleic acid-binding proteins of the Sac10b family, also known as Alba, are widely distributed in Archaea. However, the physiological roles of these proteins have yet to be clarified. Here, we show that Sis10b, a member of the Sac10b family from the hyperthermophilic archaeon Sulfolobus islandicus, was active in RNA strand exchange, duplex RNA unwinding in vitro and RNA unfolding in a heterologous host cell. This protein exhibited temperature-dependent binding preference for ssRNA over dsRNA and was more efficient in RNA unwinding and RNA unfolding at elevated temperatures. Notably, alanine substitution of a highly conserved basic residue (K) at position 17 in Sis10b drastically reduced the ability of this protein to catalyse RNA strand exchange and RNA unwinding. Additionally, the preferential binding of Sis10b to ssRNA also depended on the presence of K17 or R17. Furthermore, normal growth was restored to a slow-growing Sis10b knockdown mutant by overproducing wild-type Sis10b but not by overproducing K17A in this mutant strain. Our results indicate that Sis10b is an RNA chaperone that likely functions most efficiently at temperatures optimal for the growth of S. islandicus, and K17 is essential for the chaperone activity of the protein.

scholarly journals Neural-cadherin expression associated with angiogenesis in non-small-cell lung cancer patients

2003 ◽  
Vol 88 (11) ◽  
pp. 1727-1733 ◽  
Author(s):  
T Nakashima ◽  
C Huang ◽  
D Liu ◽  
K Kameyama ◽  
D Masuya ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Small Cell Lung Cancer ◽  
Cancer Patients ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Small Cell Lung ◽  
Lung Cancer Patients ◽  
Neural Cadherin

scholarly journals An aromatic, but not a basic, residue is involved in the toxicity of group-II phospholipase A2 neurotoxins

1999 ◽  
Vol 341 (1) ◽  
pp. 139-145 ◽  
Author(s):  
Jože PUNGERĆAR ◽  
Igor KRIAJ ◽  
Ning-Sheng LIANG ◽  
Franc GUBENŠEK
Keyword(s):  
Bovine Brain ◽  
Enzymic Activity ◽  
Aliphatic Chain ◽  
Wild Type ◽  
Basic Residue ◽  
Enzyme Active Site ◽  
Single Mutant ◽  
Adsorption Surface ◽  
Interfacial Adsorption ◽  
Triton X

Ammodytoxins (Atxs) A, B and C are basic phospholipase A2s from Vipera ammodytes ammodytes snake venom, and they exhibit presynaptic toxicity. The most toxic is AtxA, followed by AtxC, its naturally occurring F124 → I/K128 → E mutant, which is 17 times less toxic. Two mutants of AtxA have been produced in bacteria and characterized. The specific enzymic activity of the K128 → E mutant on mixed phosphatidylcholine/Triton X-100 micelles is similar to that of the wild type. The K108 → N/K111 → N mutant, however, possesses 160% of the wild-type activity. Replacement of the two basic residues by uncharged, polar residues on the opposite side of the protein to the enzyme active site and interfacial adsorption surface results in increased enzymic activity at the water/lipid aggregate interface, due to a redistribution of electrostatic charge. The binding affinity of the double mutant for the specific acceptor in bovine brain was similar to that of AtxA, whereas the affinity of the single mutant was similar to that of AtxC, which was slightly weaker than that of AtxA. Interestingly, the substitution of any of these three basic surface residues did not significantly change the lethal potency of AtxA. Since the single mutant AtxA(K128 → E) is equivalent to the AtxC(I124 → F) mutant, this indicates that the residue at position 124 is important for presynaptic toxicity of Atxs. The more than 10-fold lower toxicity of AtxC, compared with AtxA, is a consequence of the substitution of Phe-124 (aromatic ring) with Ile (aliphatic chain). Exposed aromatic residues in the C-terminal region may also be important for the neurotoxicity of other similar toxins.

scholarly journals Influence of Basic Residue Content on Fragment Ion Peak Intensities in Low-Energy Collision-Induced Dissociation Spectra of Peptides

2004 ◽  
Vol 76 (5) ◽  
pp. 1243-1248 ◽  
Author(s):  
David L. Tabb ◽  
Yingying Huang ◽  
Vicki H. Wysocki ◽  
John R. Yates
Keyword(s):  
Low Energy ◽  
Collision Induced Dissociation ◽  
Energy Collision ◽  
Basic Residue
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