scholarly journals El dominio STK de la proteína de resistencia a la bacteriosis vascular de yuca RXAM1 interactúa con una E3 Ubiquitin Ligasa

2019 ◽  
Vol 24 (1) ◽  
pp. 139-149
Author(s):  
Juliana Gil ◽  
Camilo Ernesto López Carrascal
Keyword(s):  
Manihot Esculenta ◽  
Ring Finger ◽  
E3 Ligase ◽  
Xanthomonas Axonopodis ◽  
Leucine Rich Repeats ◽  
Zinc Ribbon

La yuca (Manihot esculenta) representa el pilar de la seguridad alimentaria para cerca de mil millones de personas, principalmente en las zonas tropicales. Uno de los factores limitantes de la producción de yuca es la bacteriosis vascular causada por la bacteria Xanthomonas axonopodis pv. manihotis (Xam). Recientemente se identificó el gen RXam1 el cual confiere resistencia parcial de yuca a cepas de Xam. RXam1 codifica una proteína con un dominio LRR (Leucine Rich Repeats) extracelular y un dominio STK (Serina Treonina Kinasa) citoplasmático; estas proteínas son conocidas como RLKs (Receptor Like Kinases). En este estudio se realizó el tamizaje de una librería de ADNc de yuca mediante doble híbrido de levadura para identificar las posibles proteínas que interactúan con el dominio STK de RXam1. El tamizaje de 3x108 clones permitió identificar y confirmar cinco clones de ellos los cuales corresponden al mismo gen, el cual codifica para una proteína que presenta un dominio central de dedos de zinc CHY, seguido por un dominio C-terminal “RING finger” y un “Zinc ribbon” el cual fue denominado CRFE3-1 (Cassava RING Finger E3 ligase). La interacción entre STK y CRFE3-1 fue altamente especifica ya que se demostró también por doble híbrido que STK no interactúa con una E3 ligasa de Arabidopsis, altamente similar a CRFE3-1, así como tampoco CRFE3-1 interactúa con el dominio STK de un RLK de lechuga similar a RXam1. La identificación de CRFE3-1 sugiere que mecanismos de degradación proteica son importantes para regular la actividad de RXam1.

A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis through interaction with BNip1

2013 ◽  
Vol 25 (11) ◽  
pp. 2320-2333 ◽  
Author(s):  
Peng Wang ◽  
Yanfang Wu ◽  
Yan Li ◽  
Jiyan Zheng ◽  
Jie Tang
Keyword(s):  
Er Stress ◽  
Ring Finger ◽  
E3 Ligase

Xanthomonas axonopodis pv. poinsettiicola. [Distribution map].

2007 ◽  
Author(s):  
Keyword(s):  
New Zealand ◽  
North America ◽  
South America ◽  
Manihot Esculenta ◽  
Euphorbia Pulcherrima ◽  
Distribution Map ◽  
Xanthomonas Axonopodis ◽  
Euphorbia Milii ◽  
New Distribution ◽  
Distribution In Europe

Abstract A new distribution map is provided for Xanthomonas axonopodis pv. poinsettiicola (Patel, Bhatt and Kulkarni) Vauterin et al. Bacteria. Hosts: croton (Codiaeum variagatum), poinsettia (Euphorbia heterophylla and Euphorbia pulcherrima), Crown-of-thorns (Euphorbia milii) and cassava (Manihot esculenta). Information is given on the geographical distribution in Europe (Germany, Italy), Asia (China (Zhejiang), Cocos Islands, India (Maharashtra), Philippines, Taiwan), North America (USA (Florida)), South America (Venezuela) and Oceana (Australia (Queensland), New Zealand).

TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase

2005 ◽  
Vol 308 (1) ◽  
pp. 146-155 ◽  
Author(s):  
Jukka Kallijärvi ◽  
Ulla Lahtinen ◽  
Riikka Hämäläinen ◽  
Marita Lipsanen-Nyman ◽  
Jorma J. Palvimo ◽  
...  
Keyword(s):  
Ring Finger ◽  
E3 Ligase ◽  
Ubiquitin E3 Ligase ◽  
Mulibrey Nanism

scholarly journals EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis

2018 ◽  
Vol 220 (1) ◽  
pp. 163-177 ◽  
Author(s):  
Joung Hun Park ◽  
Chang Ho Kang ◽  
Ganesh M. Nawkar ◽  
Eun Seon Lee ◽  
Seol Ki Paeng ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Ring Finger ◽  
E3 Ligase

Ubiquitin E3 Ligase, Tripartite Motif Protein 68 (TRIM68) Inhibits TCP-1 b Function by Proteasome-Mediated Degradation and May Overcome Imatinib-Resistance.

Blood ◽  
2009 ◽  
Vol 114 (22) ◽  
pp. 3789-3789
Author(s):  
Yasuhito Terui ◽  
Ryoko Kuniyoshi ◽  
Yuji Mishima ◽  
Yuko Mishima ◽  
Kiyohiko Hatake
Keyword(s):  
Differential Display ◽  
Ring Finger ◽  
E3 Ligase ◽  
K562 Cells ◽  
Wild Type ◽  
Mcf7 Cells ◽  
Spry Domain ◽  
Ubiquitin E3 Ligase ◽  
Imatinib Resistant

Abstract Abstract 3789 Poster Board III-725 [Background] Imatinib mesylate is effective therapy against Philadelphia chromosome-positive leukemia, but the resistance develops in all phases of the disease. The identification of new proteins induced by imatinib may lead to find the novel potent molecular targets in imatinib-resistant CML. [Methods] K562 cells were treated with or without 1 mM imatinib for 24 hours, and then differential display between them was performed. TRIM68 expression was examined by RT-PCR, and in vivo ubiquitination or sumoylation assay was performed by transfection experiment and Western blot analysis. The substrates for TRIM68 were analyzed by mass spectorometry. [Results] As the results of RNA differential display, we found that the expression of TRIM68 mRNA was increased when the K562 cells were treated with 1 mM imatinib for 24 hours. TRIM68 protein possesses a RING finger domain at its N-terminal site. Since many RING-finger proteins have been identified as E3 ligases for ubiquitination or sumoylation (Meroni G, Diez-Roux G. TRIM/RBCC, a novel class of esingle protein RING finger' E3 ubiquitin ligases. Bioessays 2005; 27: 1147-57.), we examined whether TRIM68 functions as an E3 ligase for ubiquitination or sumoylation. To examine the function of TRIM68 as an E3 ligase, wild type TRIM68 and a RING domain deletion mutant of TRIM68 (TRIM68/¢R) genes were constructed into a mammalian expression vector and they were transfected into MCF7 cells. TRIM68 had auto-ubiquitination activity but not auto-sumoylation activity on the in vivo assays, suggesting that TRIM68 can be an ubiquitin E3 ligase but not sumo ligase. Moreover, wild type TRIM68 promoted the whole ubiqutination in the cells, whereas TRIM68/¢R prevented the ubiquitination inside of the cells. To identify the TRIM68-interacting proteins, we transfected FLAG-tagged wild type TRIM68 gene or B30.2/SPRY domain of TRIM68 gene into MCF7 cells, and immunoprecipitation with FLAG-M2 agarose was performed and mass spectrometric analysis was performed. As the results, we revealed that the members of molecular chaperone T-complex polypeptide 1 (TCP-1) complex, TCP-1 b and heat shock protein 70 (HSP70) interacted with TRIM68 at the B30.2/SPRY domain. Then, we examined whether TCP-1 b is one of the substrates for TRIM68-related ubiqutination. TCP-1 b was ubiquitinated by wild type TRIM68, but not by TRIM68/¢R. Furthermore, the ubiquitination of TCP-1 b was accumulated by the treatment with a proteasome inhibitor MG132. These suggested that TCP-1 b is one of the substrates for TRIM68. [Conclusions] We found that TRIM68 is induced by the treatment with imatinib and functions as an ubiquitin E3 ligase. Furthermore, we identified that TCP-1 b is a substrate of TRIM68. TRIM68 may inhibit the function of TCP-1 b as a chaperone by ubiquitination and proteasome-mediated degradation. TRIM68 is possible for a new target in the imatinib-resistant CML. Disclosures: No relevant conflicts of interest to declare.

scholarly journals DNA Damage Regulates UHRF1 Stability via the SCFβ-TrCPE3 Ligase

2013 ◽  
Vol 33 (6) ◽  
pp. 1139-1148 ◽  
Author(s):  
Hao Chen ◽  
Honghui Ma ◽  
Hiroyuki Inuzuka ◽  
Jianbo Diao ◽  
Fei Lan ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Damage ◽  
Tumor Recurrence ◽  
Ring Finger ◽  
E3 Ligase ◽  
Casein Kinase 1 ◽  
N Terminus ◽  
Steady State Levels ◽  
Bona Fide ◽  
Methylation Patterns

UHRF1 (ubiquitin-like, with PHD and RING finger domains 1) is a critical epigenetic player involved in the maintenance of DNA methylation patterns during DNA replication. Dysregulation of the UHRF1 level is implicated in cancer onset, metastasis, and tumor recurrence. Previous studies demonstrated that UHRF1 can be stabilized through USP7-mediated deubiquitylation, but the mechanism through which UHRF1 is ubiquitylated is still unknown. Here we show that proteasomal degradation of UHRF1 is mediated by the SCFβ-TrCPE3 ligase. Through bioinformatic and mutagenesis studies, we identified a functional DSG degron in the UHRF1 N terminus that is necessary for UHRF1 stability regulation. We further show that UHRF1 physically interacts with β-TrCP1 in a manner dependent on phosphorylation of serine 108 (S108UHRF1) within the DSG degron. Furthermore, we demonstrate that S108UHRF1phosphorylation is catalyzed by casein kinase 1 delta (CK1δ) and is important for the recognition of UHRF1 by SCFβ-TrCP. Importantly, we demonstrate that UHRF1 degradation is accelerated in response to DNA damage, coincident with enhanced S108UHRF1phosphorylation. Taken together, our data identify SCFβ-TrCPas a bona fide UHRF1 E3 ligase important for regulating UHRF1 steady-state levels both under normal conditions and in response to DNA damage.

804 EDEM3 Controls NEUROGENIN-3 Protein's Half-Life by Inhibiting a Specific Ring Finger E3 Ligase, RNF128 (GRAIL), Attenuated NEUROG3 Degradation

2016 ◽  
Vol 150 (4) ◽  
pp. S170
Author(s):  
Martin G. Martin ◽  
R. Sergio Solorzano-Vargas ◽  
Senta Georgia ◽  
Jiafang Wang ◽  
Shuping S. Wu ◽  
...  
Keyword(s):  
Half Life ◽  
Ring Finger ◽  
E3 Ligase ◽  
Neurogenin 3

AFLP assessment of genetic variability in cassava accessions (Manihot esculenta) resistant and susceptible to the cassava bacterial blight (CBB)

Genome ◽  
1999 ◽  
Vol 42 (2) ◽  
pp. 163-172 ◽  
Author(s):  
Gilda Sanchez ◽  
Silvia Restrepo ◽  
Myriam-Cristina Duque ◽  
Martin Fregene ◽  
Merideth Bonierbale ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Manihot Esculenta ◽  
Bacterial Blight ◽  
Multiple Correspondence Analysis ◽  
Aflp Analysis ◽  
Resistance Screening ◽  
Base Resistance ◽  
Cassava Bacterial Blight ◽  
Xanthomonas Axonopodis ◽  
Cassava Varieties

Cassava bacterial blight (CBB) is caused by Xanthomonas axonopodis pv. manihotis (Xam). Resistance is found in Manihot esculenta and, in addition, has been introgressed from a wild relative, M. glaziovii. The resistance is thought to be polygenic and additively inherited. Ninety-three varieties of M. esculenta (Crantz) were assessed by AFLPs for genetic diversity and for resistance to CBB. AFLP analysis was performed using two primer combinations and a 79.2% level of polymorphism was found. The phenogram obtained showed between 74% and 96% genetic similarity among all cassava accessions analysed. The analysis permitted the unique identification of each individual. Two Xam strains were used for resistance screening. Variation in the reaction of cassava varieties to Xam strains was observed for all plant accessions. The correlation of resistance to both strains, had a coefficient of 0.53, suggesting the independence of resistance to each strain. Multiple correspondence analysis showed a random distribution of the resistance/susceptibility response with respect to overall genetic diversity as measured by AFLP analysis. A total heterozygosity index was calculated to determine the diversity within clusters as well as among them. Our results demonstrate that resistance to CBB is broadly distributed in cassava germplasm and that AFLP analysis is an effective and efficient means of providing quantitative estimates of genetic similarities among cassava accessions.Key words: amplified fragment length polymorphism, genetic base, resistance screening, Xanthomonas axonopodis pv. manihotis.

scholarly journals Author response: RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate immunity

2016 ◽  
Author(s):  
Alison C McKelvey ◽  
Travis B Lear ◽  
Sarah R Dunn ◽  
John Evankovich ◽  
James D Londino ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Ring Finger ◽  
E3 Ligase ◽  
Author Response ◽  
Tlr2 Signaling
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