Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5

Biochemistry ◽  
2015 ◽  
Vol 54 (30) ◽  
pp. 4672-4682 ◽  
Author(s):  
Indu R. Chandrashekaran ◽  
Biswaranjan Mohanty ◽  
Edmond M. Linossi ◽  
Laura F. Dagley ◽  
Eleanor W. W. Leung ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Interaction Region ◽  
Intrinsically Disordered ◽  
N Terminus

scholarly journals Functional Characterization of the Interaction of Ste50p with Ste11p MAPKKK inSaccharomyces cerevisiae

1999 ◽  
Vol 10 (7) ◽  
pp. 2425-2440 ◽  
Author(s):  
Cunle Wu ◽  
Ekkehard Leberer ◽  
David Y. Thomas ◽  
Malcolm Whiteway
Keyword(s):  
Protein Kinase ◽  
Functional Characterization ◽  
Hog Pathway ◽  
C Terminus ◽  
Extracellular Signal ◽  
Osmotic Stress Response ◽  
N Terminus

The Saccharomyces cerevisiae Ste11p protein kinase is a homologue of mammalian MAPK/extracellular signal-regulated protein kinase kinase kinases (MAPKKKs or MEKKs) as well as theSchizosaccharomyces pombe Byr2p kinase. Ste11p functions in several signaling pathways, including those for mating pheromone response and osmotic stress response. The Ste11p kinase has an N-terminal domain that interacts with other signaling molecules to regulate Ste11p function and direct its activity in these pathways. One of the Ste11p regulators is Ste50p, and Ste11p and Ste50p associate through their respective N-terminal domains. This interaction relieves a negative activity of the Ste11p N terminus, and removal of this negative function is required for Ste11p function in the high-osmolarity glycerol (HOG) pathway. The Ste50p/Ste11p interaction is also important (but not essential) for Ste11p function in the mating pathway; in this pathway binding of the Ste11p N terminus with both Ste50p and Ste5p is required, with the Ste5p association playing the major role in Ste11p function. In vitro, Ste50p disrupts an association between the catalytic C terminus and the regulatory N terminus of Ste11p. In addition, Ste50p appears to modulate Ste11p autophosphorylation and is itself a substrate of the Ste11p kinase. Therefore, both in vivo and in vitro data support a role for Ste50p in the regulation of Ste11p activity.

scholarly journals Spectroscopic and Functional Characterization of Nitrophorin 7 from the Blood-Feeding InsectRhodnius prolixusReveals an Important Role of Its Isoform-Specific N-Terminus for Proper Protein Function†

Biochemistry ◽  
2007 ◽  
Vol 46 (46) ◽  
pp. 13254-13268 ◽  
Author(s):  
Markus Knipp ◽  
Fei Yang ◽  
Robert E. Berry ◽  
Hongjun Zhang ◽  
Maxim N. Shokhirev ◽  
...  
Keyword(s):  
Protein Function ◽  
Functional Characterization ◽  
Blood Feeding ◽  
N Terminus

scholarly journals Functional Characterization of Pepper Vein Banding Virus-Encoded Proteins and Their Interactions: Implications in Potyvirus Infection

Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 1037
Author(s):  
Pallavi Sabharwal ◽  
Handanahal S. Savithri
Keyword(s):  
Life Cycle ◽  
Functional Characterization ◽  
Distinct Species ◽  
Multifunctional Proteins ◽  
Intrinsically Disordered ◽  
Interaction Partners ◽  
Encoded Proteins ◽  
Potential Applications ◽  
Intracellular Fate

Pepper vein banding virus (PVBV) is a distinct species in the Potyvirus genus which infects economically important plants in several parts of India. Like other potyviruses, PVBV encodes multifunctional proteins, with several interaction partners, having implications at different stages of the potyviral infection. In this review, we summarize the functional characterization of different PVBV-encoded proteins with an emphasis on their interaction partners governing the multifunctionality of potyviral proteins. Intrinsically disordered domains/regions of these proteins play an important role in their interactions with other proteins. Deciphering the function of PVBV-encoded proteins and their interactions with cognitive partners will help in understanding the putative mechanisms by which the potyviral proteins are regulated at different stages of the viral life-cycle. This review also discusses PVBV virus-like particles (VLPs) and their potential applications in nanotechnology. Further, virus-like nanoparticle-cell interactions and intracellular fate of PVBV VLPs are also discussed.

scholarly journals Telomere length regulation by Rif1 protein from Hansenula polymorpha

2021 ◽  
Author(s):  
Alexander N. Malyavko ◽  
Olga A. Petrova ◽  
Maria I. Zvereva ◽  
Vladimir Polshakov ◽  
Olga A. Dontsova
Keyword(s):  
Telomere Length ◽  
Yeast Species ◽  
Hansenula Polymorpha ◽  
Functional Characterization ◽  
Strand Break ◽  
Telomere Elongation ◽  
Intrinsically Disordered ◽  
Length Regulation ◽  
Telomere Length Regulation

Rif1 is a large multifaceted protein involved in various processes of DNA metabolism – from telomere length regulation and replication to double-strand break repair. The mechanistic details of its action, however, are often poorly understood. Here, we report functional characterization of the Rif1 homologue from methylotrophic thermotolerant budding yeast Hansenula polymorpha DL-1. We show that, similar to other yeast species, H. polymorpha Rif1 suppresses telomerase-dependent telomere elongation. We uncover two novel modes of Rif1 recruitment at H. polymorpha telomeres: via direct DNA binding and through the association with the Ku heterodimer. Both of these modes (at least partially) require the intrinsically disordered N-terminal extension – a region of the protein present exclusively in yeast species. We also demonstrate that Rif1 binds Stn1 and promotes its accumulation at telomeres in H. polymorpha.

scholarly journals Structural Characterization of the N-Terminus of CRGA: An Intrinsically Disordered Region and Short β Strands to Stabilize Dimerization

2018 ◽  
Vol 114 (3) ◽  
pp. 22a
Author(s):  
Yiseul Shin ◽  
Riqiang Fu ◽  
Huajun Qin ◽  
Joshua Taylor ◽  
Malini R. Rajagopalan ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Intrinsically Disordered ◽  
N Terminus ◽  
Intrinsically Disordered Region

scholarly journals Evaluation of the Reactivity and Receptor Competition of HLA-G Isoforms toward Available Antibodies: Implications of Structural Characteristics of HLA-G Isoforms

2019 ◽  
Vol 20 (23) ◽  
pp. 5947 ◽  
Author(s):  
Atsushi Furukawa ◽  
Manami Meguro ◽  
Rika Yamazaki ◽  
Hiroshi Watanabe ◽  
Ami Takahashi ◽  
...  
Keyword(s):  
Dissociation Constants ◽  
Splice Variants ◽  
Structural Characteristics ◽  
Functional Characterization ◽  
Detection Systems ◽  
Intrinsically Disordered ◽  
Checkpoint Molecule ◽  
Maternal Immune Response ◽  
Insight Into

The human leucocyte antigen (HLA)-G, which consists of seven splice variants, is a tolerogenic immune checkpoint molecule. It plays an important role in the protection of the fetus from the maternal immune response by binding to inhibitory receptors, including leukocyte Ig-like receptors (LILRs). Recent studies have also revealed that HLA-G is involved in the progression of cancer cells and the protection from autoimmune diseases. In contrast to its well characterized isoform, HLA-G1, the binding activities of other major HLA-G isoforms, such as HLA-G2, toward available anti-HLA-G antibodies are only partially understood. Here, we investigate the binding specificities of anti-HLA-G antibodies by using surface plasmon resonance. MEM-G9 and G233 showed strong affinities to HLA-G1, with a nM range for their dissociation constants, but did not show affinities to HLA-G2. The disulfide-linker HLA-G1 dimer further exhibited significant avidity effects. On the other hand, 4H84 and MEM-G1, which can be used for the Western blotting of HLA-G isoforms, can bind to native HLA-G2, while MEM-G9 and G233 cannot. These results reveal that HLA-G2 has a partially intrinsically disordered structure. Furthermore, MEM-G1, but not 4H84, competes with the LILRB2 binding of HLA-G2. These results provide novel insight into the functional characterization of HLA-G isoforms and their detection systems.

scholarly journals A phospho-switch in the N-terminus of NRT2.1 affects nitrate uptake by controlling the interaction of NRT2.1 with NAR2.1

2020 ◽  
Author(s):  
Zhi Li ◽  
Xu Na Wu ◽  
Aurore Jaquot ◽  
Larence Lejay ◽  
Waltraud X Schulze
Keyword(s):  
Nitrate Uptake ◽  
Functional Characterization ◽  
Kinase Domain ◽  
Data Sets ◽  
C Terminus ◽  
N Terminus ◽  
Switch Mechanism ◽  
A Site ◽  
Nitrate Starvation

AbstractNRT2.1 can be phosphorylated at five different sites within N- and C-terminus. Here, we provide a systematic functional characterization of phosphorylation at S21 and S28 within the N-terminus of NRT2.1. We used existing phosphoproteomic data sets of nitrate starvation and nitrate resupply to construct a site-specific correlation network identifying kinase candidates to phosphorylate NRT2.1. By this approach, we identified NITRATE UPTAKE REGULATORY KINASE 1 (AT5G49770) which itself was regulated by phosphorylation at S839 and S870 within its kinase domain. In the active state, when S839 was dephosphorylated and S870 was phosphorylated, NURK1 was found to interact with NRT2.1 at dephosphorylated S28. Upon that interaction, NURK1 can phosphorylate NRT2.1 at S21. Phosphorylation of NRT2.1 at S21 resulted in low interaction of NRT2.1 with its activator protein NAR2.1. By contrast, phosphorylation of NRT2.1 at S28 by a yet unknown kinase enhanced the interaction with NAR2.1, but inhibited the interaction with NURK1. We propose that serines S21 and S28 are involved in a phospho-switch mechanism and by which the interaction of NRT2.1 with its activator NAR2.1, and thus NRT2.1 activity, is modulated. NURK1 here was identified as the kinase affecting this phospho-switch through phosphorylation of NRT2.1 at S21 leading to inactivation of NRT2.1.

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