In vitro characterization of the cysteine-rich capping domains in a plant leucine rich repeat protein

2006 ◽  
Vol 1764 (6) ◽  
pp. 1043-1053 ◽  
Author(s):  
Olatomirin O. Kolade ◽  
Vicki A. Bamford ◽  
Gema Ancillo Anton ◽  
Jonathan D.G. Jones ◽  
Pablo Vera ◽  
...  
Keyword(s):  
Leucine Rich Repeat ◽  
Repeat Protein ◽  
In Vitro Characterization ◽  
Leucine Rich Repeat Protein

scholarly journals Multiple Functions of the Leucine-Rich Repeat Protein LrrA of Treponema denticola

2004 ◽  
Vol 72 (8) ◽  
pp. 4619-4627 ◽  
Author(s):  
Akihiko Ikegami ◽  
Kiyonobu Honma ◽  
Ashu Sharma ◽  
Howard K. Kuramitsu
Keyword(s):  
Tandem Repeats ◽  
Specific Binding ◽  
Treponema Denticola ◽  
Binding Motif ◽  
Strain Atcc ◽  
Leucine Rich Repeat ◽  
Repeat Protein ◽  
Tannerella Forsythensis ◽  
Leucine Rich Repeat Protein

ABSTRACT The gene lrrA, encoding a leucine-rich repeat protein, LrrA, that contains eight consensus tandem repeats of 23 amino acid residues, has been identified in Treponema denticola ATCC 35405. A leucine-rich repeat is a generally useful protein-binding motif, and proteins containing this repeat are typically involved in protein-protein interactions. Southern blot analysis demonstrated that T. denticola ATCC 35405 expresses the lrrA gene, but the gene was not identified in T. denticola ATCC 33520. In order to analyze the functions of LrrA in T. denticola, an lrrA-inactivated mutant of strain ATCC 35405 and an lrrA gene expression transformant of strain ATCC 33520 were constructed. Characterization of the mutant and transformant demonstrated that LrrA is associated with the extracytoplasmic fraction of T. denticola and expresses multifunctional properties. It was demonstrated that the attachment of strain ATCC 35405 to HEp-2 cell cultures and coaggregation with Tannerella forsythensis were attenuated by the lrrA mutation. In addition, an in vitro binding assay demonstrated specific binding of LrrA to a portion of the Tannerella forsythensis leucine-rich repeat protein, BspA, which is mediated by the N-terminal region of LrrA. It was also observed that the lrrA mutation caused a reduction of swarming in T. denticola ATCC 35405 and consequently attenuated tissue penetration. These results suggest that the leucine-rich repeat protein LrrA plays a role in the attachment and penetration of human epithelial cells and coaggregation with Tannerella forsythensis. These properties may play important roles in the virulence of T. denticola.

scholarly journals Nuclear Localization Leucine-Rich-Repeat Protein 1 Deficiency Protects Against Cardiac Hypertrophy by Pressure Overload

2018 ◽  
Vol 48 (1) ◽  
pp. 75-86 ◽  
Author(s):  
Jing Zong ◽  
Fang-fang Li ◽  
Kai Liang ◽  
Rui Dai ◽  
Hao Zhang ◽  
...  
Keyword(s):  
Cardiac Hypertrophy ◽  
Nuclear Localization ◽  
Neonatal Rat ◽  
Cardiomyocyte Hypertrophy ◽  
Leucine Rich Repeat ◽  
Aortic Banding ◽  
Rat Cardiomyocytes ◽  
Repeat Protein ◽  
Leucine Rich Repeat Protein

Background/Aims: Nuclear localization leucine-rich-repeat protein 1 (NLRP1) is a cytoplasmic protein, involved in autoimmune diseases, mammalian reproduction, neuronal cell death, and stroke. However, the role of NLRP1 in cardiac hypertrophy remains unclear. We used in vivo and in vitro models to investigate the effects of NLRP1 on cardiac hypertrophy. Methods: We used NLRP1-deficient mice and cultured neonatal rat cardiomyocytes with gain and loss of NLRP1 function. Cardiac hypertrophy was estimated by echocardiographic and hemodynamic measurements, and by pathological and molecular analysis. Results: Eight weeks after aortic banding (AB), NLRP1 deficiency significantly inhibited aortic banding–induced cardiac hypertrophy, inflammation, and fibrosis. Activation of MAPK, NF-κB, and TGF-β/Smad pathways was reduced in NLRP1-knockout (KO) mice compared with that in wild-type (WT) mice. Consistent with these results, in vitro studies, performed using cultured neonatal mouse cardiomyocytes, confirmed that NLRP1 deficiency protects against cardiomyocyte hypertrophy induced by isoproterenol (PE); this protective activity was associated with the arrest of MAPK and NF-κB signaling. Conclusions: Our data illustrates that NLRP1 plays a crucial role in the development of cardiac hypertrophy via positive regulation of the MAPK, NF-κB, and TGF-β/Smad signaling pathways.

scholarly journals Functional characterization of podocan, a member of a new class in the small leucine-rich repeat protein family

FEBS Letters ◽  
2004 ◽  
Vol 563 (1-3) ◽  
pp. 69-74 ◽  
Author(s):  
Ryoko Shimizu-Hirota ◽  
Hiroyuki Sasamura ◽  
Mari Kuroda ◽  
Emi Kobayashi ◽  
Takao Saruta
Keyword(s):  
Functional Characterization ◽  
Protein Family ◽  
Leucine Rich Repeat ◽  
Repeat Protein ◽  
New Class ◽  
Leucine Rich Repeat Protein

scholarly journals Characterization of a novel anther-specific gene encoding a leucine-rich repeat protein in petunia

2014 ◽  
Vol 13 (4) ◽  
pp. 9889-9898 ◽  
Author(s):  
Y.Z. Yue ◽  
J. Sun ◽  
X. Huang ◽  
H. Peng ◽  
G.F. Liu ◽  
...  
Keyword(s):  
Specific Gene ◽  
Leucine Rich Repeat ◽  
Gene Encoding ◽  
Repeat Protein ◽  
Leucine Rich Repeat Protein

scholarly journals Structural and Molecular Characterization of Iron-sensing Hemerythrin-like Domain within F-box and Leucine-rich Repeat Protein 5 (FBXL5)

2012 ◽  
Vol 287 (10) ◽  
pp. 7357-7365 ◽  
Author(s):  
Joel W. Thompson ◽  
Ameen A. Salahudeen ◽  
Srinivas Chollangi ◽  
Julio C. Ruiz ◽  
Chad A. Brautigam ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Leucine Rich Repeat ◽  
Repeat Protein ◽  
Leucine Rich Repeat Protein
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