scholarly journals A Single Protein S-acyl Transferase Acts through Diverse Substrates to Determine Cryptococcal Morphology, Stress Tolerance, and Pathogenic Outcome

2015 ◽  
Vol 11 (5) ◽  
pp. e1004908 ◽  
Author(s):  
Felipe H. Santiago-Tirado ◽  
Tao Peng ◽  
Meng Yang ◽  
Howard C. Hang ◽  
Tamara L. Doering
Keyword(s):  
Stress Tolerance ◽  
Protein S ◽  
Acyl Transferase ◽  
Single Protein

scholarly journals Dynamic Protein S-Acylation in Plants

2019 ◽  
Vol 20 (3) ◽  
pp. 560 ◽  
Author(s):  
Lihua Zheng ◽  
Peng Liu ◽  
Qianwen Liu ◽  
Tao Wang ◽  
Jiangli Dong
Keyword(s):  
Protein S ◽  
Acyl Transferase ◽  
Lipid Modification ◽  
Post Translational Modification ◽  
Lipid Modifications ◽  
Acylated Proteins

Lipid modification is an important post-translational modification. S-acylation is unique among lipid modifications, as it is reversible and has thus attracted much attention. We summarize some proteins that have been shown experimentally to be S-acylated in plants. Two of these S-acylated proteins have been matched to the S-acyl transferase. More importantly, the first protein thioesterase with de-S-acylation activity has been identified in plants. This review shows that S-acylation is important for a variety of different functions in plants and that there are many unexplored aspects of S-acylation in plants.

scholarly journals Protein S-acyl transferase 15 is involved in seed triacylglycerol catabolism during early seedling growth in Arabidopsis

2019 ◽  
Vol 70 (19) ◽  
pp. 5205-5216 ◽  
Author(s):  
Yaxiao Li ◽  
Jianfeng Xu ◽  
Gang Li ◽  
Si Wan ◽  
Oliver Batistič ◽  
...  
Keyword(s):  
Seedling Growth ◽  
Seed Storage ◽  
Protein S ◽  
Acyl Transferase ◽  
Early Seedling Growth ◽  
Early Seedling ◽  
Growth Of Seedlings

Protein S-acyl transferase 15 is involved in β-oxidation of seed-storage triacylglycerol in Arabidopsis, which is required to provide sugars for normal post-germination growth of seedlings.

scholarly journals Both male and female gametogenesis require a fully functional protein S‐ acyl transferase 21 in Arabidopsis thaliana

2019 ◽  
Vol 100 (4) ◽  
pp. 754-767 ◽  
Author(s):  
Yaxiao Li ◽  
Hong‐Ju Li ◽  
Chris Morgan ◽  
Kirsten Bomblies ◽  
Weicai Yang ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Protein S ◽  
Acyl Transferase ◽  
Functional Protein ◽  
Male And Female ◽  
Female Gametogenesis

Orientation of actin filaments during motion in motility assay

1995 ◽  
Vol 53 ◽  
pp. 52-53
Author(s):  
J. Borejdo ◽  
S. Burlacu
Keyword(s):  
Actin Filaments ◽  
Thin Filament ◽  
Striated Muscle ◽  
Myosin Head ◽  
Classical Method ◽  
Polarization Of Fluorescence ◽  
Single Protein ◽  
Intracellular Organelles ◽  
Change Orientation ◽  
Active Entity

Polarization of fluorescence is a classical method to assess orientation or mobility of macromolecules. It has been a common practice to measure polarization of fluorescence through a microscope to characterize orientation or mobility of intracellular organelles, for example anisotropic bands in striated muscle. Recently, we have extended this technique to characterize single protein molecules. The scientific question concerned the current problem in muscle motility: whether myosin heads or actin filaments change orientation during contraction. The classical view is that the force-generating step in muscle is caused by change in orientation of myosin head (subfragment-1 or SI) relative to the axis of thin filament. The molecular impeller which causes this change resides at the interface between actin and SI, but it is not clear whether only the myosin head or both SI and actin change orientation during contraction. Most studies assume that observed orientational change in myosin head is a reflection of the fact that myosin is an active entity and actin serves merely as a passive "rail" on which myosin moves.

Projected Structure of the Surface Protein of Sulfolobus Spec. B12 Determined to a Resolution of 1.0 NM by Cryo-Electronmicroscopy

1990 ◽  
Vol 48 (1) ◽  
pp. 102-103
Author(s):  
G. Lembcke ◽  
F. Zemlin
Keyword(s):  
Low Dose ◽  
Maximum Dose ◽  
Three Dimensional ◽  
Surface Protein ◽  
Protein S ◽  
Radiation Sensitivity ◽  
Specimen Preparation ◽  
Molecular Architecture ◽  
High Radiation ◽  
Fritz Haber

The thermoacidophilic archaebacterium Sulfolobus spec. B12 , which is closely related to Sulfolobus solfataricus , possesses a regularly arrayed surface protein (S-layer), which is linked to the plasma membrane via spacer elements spanning a distinct interspace of approximately 18 nm. The S-layer has p3-Symmetry and a lattice constant of 21 nm; three-dimensional reconstructions of negatively stained fragments yield a layer thickness of approximately 6-7 nm.For analysing the molecular architecture of Sulfolobus surface protein in greater detail we use aurothioglucose(ATG)-embedding for specimen preparation. Like glucose, ATG, is supposed to mimic the effect of water, but has the advantage of being less volatile. ATG has advantages over glucose when working with specimens composed exclusively of protein because of its higher density of 2.92 g cm-3. Because of its high radiation sensitivity electromicrographs has to be recorded under strict low-dose conditions. We have recorded electromicrographs with a liquid helium-cooled superconducting electron microscope (the socalled SULEIKA at the Fritz-Haber-lnstitut) with a specimen temperature of 4.5 K and with a maximum dose of 2000 e nm-2 avoiding any pre-irradiation of the specimen.

Investigating stress tolerance as a predictor of multitasking performance

2009 ◽  
Author(s):  
Ted B. Kinney ◽  
Mei-Chuan Kung ◽  
Kathleen M. Meckley ◽  
Kristin M. Delgado
Keyword(s):  
Stress Tolerance
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