Synthesis of cyclopsychotride by orthogonal ligation using unprotected peptide precursor

2005 ◽  
pp. 229-230
Author(s):  
Yi-An Lu ◽  
James P. Tam
Keyword(s):  
Peptide Precursor

Precursor processing by SBT3.8 and phytosulfokine signaling contribute to drought stress tolerance in Arabidopsis

2021 ◽  
Author(s):  
Nils Stührwohldt ◽  
Eric Bühler ◽  
Margret Sauter ◽  
Andreas Schaller
Keyword(s):  
Drought Stress ◽  
Osmotic Stress ◽  
Stress Tolerance ◽  
Serine Proteases ◽  
Loss Of Function ◽  
Lateral Root Development ◽  
Osmotic Stress Tolerance ◽  
Stress Symptoms ◽  
C Terminus ◽  
Peptide Precursor

Abstract Increasing drought stress poses a severe threat to agricultural productivity. Plants, however, evolved numerous mechanisms to cope with such environmental stress. Here we report that the stress-induced production of a peptide signal contributes to stress tolerance. The expression of phytosulfokine (PSK) peptide precursor genes, and transcripts of three subtilisin-like serine proteases, SBT1.4, SBT3.7 and SBT3.8 were found to be up-regulated in response to osmotic stress. Stress symptoms were enhanced in sbt3.8 loss-of-function mutants and could be alleviated by PSK treatment. Osmotic stress tolerance was improved in plants overexpressing the precursor of PSK1 (proPSK1) or SBT3.8 resulting in higher fresh weight and improved lateral root development in the transgenic compared to wild-type plants. We further showed that SBT3.8 is involved in the biogenesis of the bioactive PSK peptide. ProPSK1 was cleaved by SBT3.8 at the C-terminus of the PSK pentapeptide. Processing by SBT3.8 depended on the aspartic acid residue directly following the cleavage site. ProPSK1 processing was impaired in the sbt3.8 mutant. The data suggest that increased expression in response to osmotic stress followed by the post-translational processing of proPSK1 by SBT3.8 leads to the production of PSK as a peptide signal for stress mitigation.

scholarly journals Purification and tissue level of the beta-amyloid peptide precursor of rat brain

1991 ◽  
Vol 266 (13) ◽  
pp. 8464-8469
Author(s):  
A. Potempska ◽  
J. Styles ◽  
P. Mehta ◽  
K.S. Kim ◽  
D.L. Miller
Keyword(s):  
Rat Brain ◽  
Beta Amyloid ◽  
Tissue Level ◽  
Amyloid Peptide ◽  
Beta Amyloid Peptide ◽  
Peptide Precursor

Expression and clinical value of gastrin‐releasing peptide precursor in nephropathy and chronic kidney disease

Nephrology ◽  
2020 ◽  
Vol 25 (5) ◽  
pp. 398-405
Author(s):  
Zhang Dai ◽  
Jianhui Zhu ◽  
Huibin Huang ◽  
Lili Fang ◽  
Yongzhi Lin ◽  
...  
Keyword(s):  
Chronic Kidney Disease ◽  
Kidney Disease ◽  
Clinical Value ◽  
Gastrin Releasing Peptide ◽  
Peptide Precursor

Cysteine as peptide precursor and catalyst

Science ◽  
2020 ◽  
Vol 370 (6518) ◽  
pp. 805.15-807
Author(s):  
Michael A. Funk
Keyword(s):  
Peptide Precursor

The Structural Gene for Microcin H47 Encodes a Peptide Precursor with Antibiotic Activity

1999 ◽  
Vol 43 (9) ◽  
pp. 2176-2182 ◽  
Author(s):  
Eliana Rodríguez ◽  
Carina Gaggero ◽  
Magela Laviña
Keyword(s):  
Escherichia Coli ◽  
Gene Fusion ◽  
Genetic System ◽  
Antibiotic Activity ◽  
Peptide Antibiotic ◽  
Bifunctional Protein ◽  
Naturally Occurring ◽  
Hydrophobic Peptide ◽  
Peptide Precursor ◽  
Highly Hydrophobic

ABSTRACT Microcin H47 is a bactericidal antibiotic produced by a naturally occurring Escherichia coli strain isolated in Uruguay. The microcin genetic system is located in the chromosome and extends over a 10-kb DNA segment containing the genes required for microcin synthesis, secretion, and immunity. The smallest microcin synthesis gene,mchB, was sequenced and shown to encode a highly hydrophobic peptide. An mchB-phoA gene fusion, which directed the synthesis of a hybrid bifunctional protein with both PhoA and microcin H47-like activities, was isolated. The results presented herein lead us to propose that microcin H47 is indeed a ribosomally synthesized peptide antibiotic and that its peptide precursor already has antibiotic activity of the same specificity as that of mature microcin.

Structure and analysis of the bovine atrial natriuretic peptide precursor gene

1986 ◽  
Vol 136 (1) ◽  
pp. 396-403 ◽  
Author(s):  
George P. Vlasuk ◽  
Judith Miller ◽  
Gerard H. Bencen ◽  
John A. Lewicki
Keyword(s):  
Atrial Natriuretic Peptide ◽  
Natriuretic Peptide ◽  
Peptide Precursor ◽  
Atrial Natriuretic
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