scholarly journals Correction: Chain release mechanisms in polyketide and non-ribosomal peptide biosynthesis

2021 ◽  
Author(s):  
Rory F. Little ◽  
Christian Hertweck
Keyword(s):  
Release Mechanisms ◽  
Peptide Biosynthesis

Correction for ‘Chain release mechanisms in polyketide and non-ribosomal peptide biosynthesis’ by Rory F. Little et al., Nat. Prod. Rep., 2021, DOI: 10.1039/d1np00035g.

scholarly journals Chain release mechanisms in polyketide and non-ribosomal peptide biosynthesis

2021 ◽  
Author(s):  
Rory F. Little ◽  
Christian Hertweck
Keyword(s):  
Release Mechanisms ◽  
Peptide Biosynthesis

This review covers the mechanisms of chain release in polyketide and non-ribosomal peptide biosynthesis.

scholarly journals Experimental CanSat Platform for Functional Verification of Burn Wire Triggering-Based Holding and Release Mechanisms

Aerospace ◽  
2021 ◽  
Vol 8 (7) ◽  
pp. 192
Author(s):  
Shankar Bhattarai ◽  
Ji-Seong Go ◽  
Hyun-Ung Oh
Keyword(s):  
Functional Performance ◽  
Flight Test ◽  
Easy Access ◽  
Functional Verification ◽  
Release Mechanism ◽  
Space Technology ◽  
Solar Panels ◽  
Distinctive Features ◽  
Release Mechanisms ◽  
Design Effectiveness

In this study, we present the Diverse Holding and Release Mechanism Can Satellite (DHRM CanSat) platform developed by the Space Technology Synthesis Laboratory (STSL) at Chosun University, South Korea. This platform focuses on several types of holding and release mechanisms (HRMs) for application in deployable appendages of nanosatellites. The objectives of the DHRM CanSat mission are to demonstrate the design effectiveness and functionality of the three newly proposed HRMs based on the burn wire triggering method, i.e., the pogo pin-type HRM, separation nut-type HRM, and Velcro tape-type HRM, which were implemented on deployable dummy solar panels of the CanSat. The proposed mechanisms have many advantages, including a high holding capability, simultaneous constraints in multi-plane directions, and simplicity of handling. Additionally, each mechanism has distinctive features, such as spring-loaded pins to initiate deployment, a plate with a thread as a nut for a high holding capability, and a hook and loop fastener for easy access to subsystems of the satellite without releasing the holding constraint. The design effectiveness and functional performance of the proposed mechanisms were demonstrated through an actual flight test of the DHRM CanSat launched by a model rocket.

Nonribosomal Peptide Biosynthesis: Point Mutations and Module Skipping Lead to Chemical Diversity

2006 ◽  
Vol 45 (14) ◽  
pp. 2296-2301 ◽  
Author(s):  
Silke C. Wenzel ◽  
Peter Meiser ◽  
Tina M. Binz ◽  
Taifo Mahmud ◽  
Rolf Müller
Keyword(s):  
Point Mutations ◽  
Chemical Diversity ◽  
Nonribosomal Peptide ◽  
Peptide Biosynthesis

AN EVALUATION OF ORDER RELEASE MECHANISMS IN A JOB-SHOP ENVIRONMENT

1988 ◽  
Vol 19 (1) ◽  
pp. 167-189 ◽  
Author(s):  
Gary L. Ragatz ◽  
Vincent A. Mabert
Keyword(s):  
Job Shop ◽  
Release Mechanisms ◽  
Order Release

scholarly journals The Contribution of Syringopeptin and Syringomycin to Virulence of Pseudomonas syringae pv. syringae strain B301D on the Basis of sypA and syrB1 Biosynthesis Mutant Analysis

2001 ◽  
Vol 14 (3) ◽  
pp. 336-348 ◽  
Author(s):  
Brenda K. Scholz-Schroeder ◽  
Michael L. Hutchison ◽  
Ingeborg Grgurina ◽  
Dennis C. Gross
Keyword(s):  
Pseudomonas Syringae ◽  
High Performance ◽  
Sweet Cherry ◽  
Peptide Structure ◽  
Acid Activation ◽  
Virulence Determinants ◽  
Amino Acid Activation ◽  
Peptide Synthetases ◽  
Peptide Synthetase ◽  
Peptide Biosynthesis

Sequencing of an approximately 3.9-kb fragment downstream of the syrD gene of Pseudomonas syringae pv. syringae strain B301D revealed that this region, designated sypA, codes for a peptide synthetase, a multifunctional enzyme involved in the thiotemplate mechanism of peptide biosynthesis. The translated protein sequence encompasses a complete amino acid activation module containing the conserved domains characteristic of peptide synthetases. Analysis of the substrate specificity region of this module indicates that it incorporates 2,3-dehydroaminobutyric acid into the syringopeptin peptide structure. Bioassay and high performance liquid chromatography data confirmed that disruption of the sypA gene in strain B301D resulted in the loss of syringopeptin production. The contribution of syringopeptin and syringomycin to the virulence of P. syringae pv. syringae strain B301D was examined in immature sweet cherry with sypA and syrB1 synthetase mutants defective in the production of the two toxins, respectively. Syringopeptin (sypA) and syringomycin (syrB1) mutants were reduced in virulence 59 and 26%, respectively, compared with the parental strain in cherry, whereas the syringopeptin-syringomycin double mutant was reduced 76% in virulence. These data demonstrate that syringopeptin and syringomycin are major virulence determinants of P. syringae pv. syringae.

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