SDS

Last update 08 May 2025

Basic Info

Synonyms

L-serine deaminase, L-serine dehydratase/L-threonine deaminase, L-threonine dehydratase

+ [4]

Introduction

Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha-ketobutyrate and pyruvate, respectively.

100 Clinical Results associated with SDS

100 Translational Medicine associated with SDS

0 Patents (Medical) associated with SDS

404

Literatures (Medical) associated with SDS

01 Feb 2025·Plant Molecular Biology

Microsporocytic ARF17 misexpression leads to an excess callose deposition and male sterility in Arabidopsis

Article

Author: Yang, Naiying ; Wang, Bo ; Huang, Jing ; Liu, Yaqi ; Chen, Yijia ; Li, Yingyin ; Su, Wenxin ; Wang, Kaiqi ; Xu, Xiaofeng

The accurate callose deposition plays important roles in pollen wall formation and pollen fertility. As a direct target of miRNA160, ARF17 participate in the formation of the callose wall. However, the impact of ARF17 misexpression in microsporocytes on callose wall formation and pollen fertility remains unknown. Here, the SDS promoter, which is capable of specifically driving gene expression in microsporocytes, was employed to drive the expression of 5mARF17. The pSDS:5mARF17#3 transgenic line were male sterile. TEM revealed that sporopollenin substance was embedded in a thicker callose layer, which resulted in the complete loss of exine structure and pollen abortion in the pSDS:5mARF17#3 line. Consistently, RT-qPCR revealed an increase in the expression of several Cals genes in pSDS:5mARF17#3. EMSA assay demonstrated that ARF17 could bind to the promoter of Cals4 gene, which further suggest that ARF17 could regulate several Cals genes expression. It is notable that the expression of several exine formation-related genes increased significantly in pSDS:5mARF17#3. In conclusion, our findings highlight that the regulation of miRNA160-ARF17 in microsporocytes modulates the thickness of the callose wall, which is crucial for pollen exine formation and intercellular communication.

01 Dec 2024·Journal of Biological Chemistry

Knotty is nice: Metabolite binding and RNA-mediated gene regulation by the preQ1 riboswitch family

Review

Author: Jenkins, Jermaine L ; Goenner, Coleman ; Srivastava, Yoshita ; Wedekind, Joseph E. ; Wedekind, Joseph E ; Schroeder, Griffin M ; Kiliushik, Daniil ; Schroeder, Griffin M. ; Jenkins, Jermaine L. ; Law, Matthew

Riboswitches sense specific cellular metabolites, leading to messenger RNA conformational changes that regulate downstream genes. Here, we review the three known prequeosine₁ (preQ₁) riboswitch classes, which encompass five gene-regulatory motifs derived from distinct consensus models of folded RNA pseudoknots. Structural and functional analyses reveal multiple gene-regulation strategies ranging from partial occlusion of the ribosome-binding Shine-Dalgarno sequence (SDS), SDS sequestration driven by kinetic or thermodynamic folding pathways, direct preQ₁ recognition by the SDS, and complete SDS burial with in the riboswitch architecture. Family members can also induce elemental transcriptional pausing, which depends on ligand-mediated pseudoknot formation. Accordingly, preQ₁ family members provide insight into a wide range of gene-regulatory tactics as well as a diverse repertoire of chemical approaches used to recognize the preQ₁ metabolite. From a broader perspective, future challenges for the field will include the identification of new riboswitches in mRNAs that do not possess an SDS or those that induce ligand-dependent transcriptional pausing. When choosing an antibacterial target, the field must also consider how well a riboswitch accommodates mutations. Investigation of riboswitches in their natural context will also be critical to elucidate how RNA-mediated gene regulation influences organism fitness, thus providing a firm foundation for antibiotic development.

01 Dec 2024·Cellular and Molecular Life Sciences

Phospholipid scramblase 1: an essential component of the nephrocyte slit diaphragm

Article

Author: Sarmiento-Jiménez, Jorge ; Castillo-Mancho, Vicente ; Culi, Joaquim ; Ruiz-Gómez, Mar ; Atienza-Manuel, Alexandra

AbstractBlood ultrafiltration in nephrons critically depends on specialized intercellular junctions between podocytes, named slit diaphragms (SDs). Here, by studying a homologous structure found in Drosophila nephrocytes, we identify the phospholipid scramblase Scramb1 as an essential component of the SD, uncovering a novel link between membrane dynamics and SD formation. In scramb1 mutants, SDs fail to form. Instead, the SD components Sticks and stones/nephrin, Polychaetoid/ZO-1, and the Src-kinase Src64B/Fyn associate in cortical foci lacking the key SD protein Dumbfounded/NEPH1. Scramb1 interaction with Polychaetoid/ZO-1 and Flotillin2, the presence of essential putative palmitoylation sites and its capacity to oligomerize, suggest a function in promoting SD assembly within lipid raft microdomains. Furthermore, Scramb1 interactors as well as its functional sensitivity to temperature, suggest an active involvement in membrane remodeling processes during SD assembly. Remarkably, putative Ca2+-binding sites in Scramb1 are essential for its activity raising the possibility that Ca2+ signaling may control the assembly of SDs by impacting on Scramb1 activity.

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