Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VI. Amino Acids with Positively Charged Side Chains:l-Lysine andl-Arginine

2010 ◽  
Vol 114 (2) ◽  
pp. 1077-1088 ◽  
Author(s):  
Belén Hernández ◽  
Fernando Pflüger ◽  
Najoua Derbel ◽  
Joël De Coninck ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides ◽  
Positively Charged

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. VIII. Amino Acids with Aromatic Side Chains:l-Phenylalanine,l-Tyrosine, andl-Tryptophan

2010 ◽  
Vol 114 (46) ◽  
pp. 15319-15330 ◽  
Author(s):  
Belén Hernández ◽  
Fernando Pflüger ◽  
Alain Adenier ◽  
Sergei G. Kruglik ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. 3. Successive KL Repeats Induce Highly Stable β-Strands Capable of Forming Non-H-Bonded Aggregates

2008 ◽  
Vol 112 (4) ◽  
pp. 1282-1289 ◽  
Author(s):  
Guy Guiffo-Soh ◽  
Belén Hernández ◽  
Yves-Marie Coïc ◽  
Fatima-Zohra Boukhalfa-Heniche ◽  
Giulia Fadda ◽  
...  
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. II. Role of KLLL Repeats To Induce Helical Conformations in Minimalist LK-Peptides

2007 ◽  
Vol 111 (43) ◽  
pp. 12563-12572 ◽  
Author(s):  
Guy Guiffo-Soh ◽  
Belén Hernández ◽  
Yves-Marie Coïc ◽  
Fatima-Zohra Boukhalfa-Heniche ◽  
Mahmoud Ghomi
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

Vibrational Analysis of Amino Acids and Short Peptides in Hydrated Media. I. L-glycine and L-leucine

2007 ◽  
Vol 111 (6) ◽  
pp. 1470-1477 ◽  
Author(s):  
Najoua Derbel ◽  
Belén Hernández ◽  
Fernando Pflüger ◽  
Jean Liquier ◽  
Frédéric Geinguenaud ◽  
...  
Keyword(s):  
Amino Acids ◽  
Vibrational Analysis ◽  
Short Peptides

scholarly journals The Superagonistic Activity of Bovine Thyroid-stimulating Hormone (TSH) and the Human TR1401 TSH Analog Is Determined by Specific Amino Acids in the Hinge Region of the Human TSH Receptor

2009 ◽  
Vol 284 (24) ◽  
pp. 16317-16324 ◽  
Author(s):  
Sandra Mueller ◽  
Gunnar Kleinau ◽  
Mariusz W. Szkudlinski ◽  
Holger Jaeschke ◽  
Gerd Krause ◽  
...  
Keyword(s):  
Amino Acids ◽  
Thyroid Stimulating Hormone ◽  
Hinge Region ◽  
Camp Production ◽  
Glycoprotein Hormone ◽  
Charged Amino Acids ◽  
Bovine Thyroid ◽  
Positively Charged ◽  
Bovine Tsh ◽  
Signaling Activity

Bovine TSH (bTSH) has a higher affinity to the human TSHR (hTSHR) and a higher signaling activity than human TSH (hTSH). The molecular reasons for these phenomena are unknown. Distinct negatively charged residues (Glu297, Glu303, and Asp382) in the hinge region of the hTSHR are known to be important for bTSH binding and signaling. To investigate the potential relevance of these positions for differences between bTSH and hTSH in the interaction to the hTSHR, we determined bTSH- and hTSH-mediated cAMP production of several substitutions at these three hinge residues. To examine specific variations of hTSH, we also investigated the superagonistic hTSH analog TR1401 (TR1401), whose sequence differs from hTSH by four additional positively charged amino acids that are also present in bTSH. To characterize possible interactions between the acidic hTSHR positions Glu297, Glu303, or Asp382 and the additional basic residues of TR1401, we investigated TR1401 binding and signaling properties. Our data reveal increased cAMP signaling of the hTSHR using TR1401 and bTSH compared with hTSH. Whereas Asp382 seems to be important for bTSH- and TR1401-mediated but not for hTSH-mediated signaling, the substitution E297K exhibits a decreased signaling for all three TSH variants. Interestingly, bTSH and TR1401 showed only a slightly different binding pattern. These observations imply that specific residues of the hinge region are mediators of the superagonistic activity of bTSH and TR1401 in contrast to hTSH. Moreover, the simultaneous localization of binding components in the glycoprotein hormone molecule and the receptor hinge region permits important reevaluation of interacting hormone receptor domains.

scholarly journals OsWRKY62 and OsWRKY76 interact with Importin α1s for Negative Regulation of Defensive Responses in Nucleus

2021 ◽  
Author(s):  
Xiaohui Xu ◽  
Han Wang ◽  
Jiqin Liu ◽  
Shuying Han ◽  
Miaomiao Lin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nuclear Localization ◽  
Nuclear Export ◽  
Nuclear Translocation ◽  
Nuclear Export Signal ◽  
Defense Responses ◽  
Nuclear Localization Signals ◽  
Defensive Responses ◽  
Export Signal ◽  
Positively Charged

Abstract Background: OsWRKY62 and OsWRKY76, two close members of WRKY transcription factors, function together as transcriptional repressors. OsWRKY62 is predominantly localized in the cytosol. What are the regulatory factors for OsWRKY62 nuclear translocation?Results: In this study, we characterized they interacted with rice importin, OsIMα1a and OsIMα1b, for nuclear translocation. Chimeric OsWRKY62.1-GFP, which is predominantly localized in the cytoplasm, was translocated to the nucleus of Nicotiana benthamiana leaf cells in the presence of OsIMα1a or OsIMαDIBB1a lacking the auto-inhibitory importin β-binding domain. OsIMαDIBB1a interacted with the WRKY domain of OsWRKY62.1, which has specific bipartite positively charged concatenated amino acids functioning as a nuclear localization signal. Similarly, we found that OsIMαDIBB1a interacted with the AvrPib effector of rice blast fungus Magnaporthe oryzae, which contains a scattered distribution of positively charged amino acids. Furthermore, we identified a nuclear export signal in OsWRKY62.1 that inhibited nuclear transportation. Overexpression of OsIMα1a or OsIMα1b enhanced resistance to M. oryzae, whereas knockout mutants decreased resistance to the pathogen. However, overexpressing both OsIMα1a and OsWRKY62.1 were slightly more susceptible to M. oryzae than OsWRKY62.1 alone. Ectopic overexpression of OsWRKY62.1 with an extra nuclear export signal compromised the enhanced susceptibility of OsWRKY62.1 to M. oryzae.Conclusion: These results indicated that OsWRKY62 localization is a consequence of competition binding between rice importins and exportins. OsWRKY62, OsWRKY76, and AvrPib effector translocate to nucleus in association with importin α1s through new types of nuclear localization signals for negatively regulating defense responses.

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