Temperature-sensitive elastin-mimetic dendrimers: Effect of peptide length and dendrimer generation to temperature sensitivity

Biopolymers ◽  
2014 ◽  
Vol 101 (6) ◽  
pp. 603-612 ◽  
Author(s):  
Chie Kojima ◽  
Kotaro Irie ◽  
Tomoko Tada ◽  
Naoki Tanaka
Keyword(s):  
Temperature Sensitivity ◽  
Temperature Sensitive ◽  
Peptide Length ◽  
Dendrimer Generation

scholarly journals A Single Point Mutation, Asn16→Lys, Dictates the Temperature-Sensitivity of the Reovirus tsG453 Mutant

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 289
Author(s):  
Kathleen K. M. Glover ◽  
Danica M. Sutherland ◽  
Terence S. Dermody ◽  
Kevin M. Coombs
Keyword(s):  
Amino Acid ◽  
Temperature Sensitivity ◽  
Reverse Genetics ◽  
Core Protein ◽  
Single Point ◽  
Single Amino Acid ◽  
Single Point Mutation ◽  
Temperature Sensitive ◽  
Amino Acid Substitutions ◽  
Gene Encoding

Studies of conditionally lethal mutants can help delineate the structure-function relationships of biomolecules. Temperature-sensitive (ts) mammalian reovirus (MRV) mutants were isolated and characterized many years ago. Two of the most well-defined MRV ts mutants are tsC447, which contains mutations in the S2 gene encoding viral core protein σ2, and tsG453, which contains mutations in the S4 gene encoding major outer-capsid protein σ3. Because many MRV ts mutants, including both tsC447 and tsG453, encode multiple amino acid substitutions, the specific amino acid substitutions responsible for the ts phenotype are unknown. We used reverse genetics to recover recombinant reoviruses containing the single amino acid polymorphisms present in ts mutants tsC447 and tsG453 and assessed the recombinant viruses for temperature-sensitivity by efficiency-of-plating assays. Of the three amino acid substitutions in the tsG453 S4 gene, Asn16-Lys was solely responsible for the tsG453ts phenotype. Additionally, the mutant tsC447 Ala188-Val mutation did not induce a temperature-sensitive phenotype. This study is the first to employ reverse genetics to identify the dominant amino acid substitutions responsible for the tsC447 and tsG453 mutations and relate these substitutions to respective phenotypes. Further studies of other MRV ts mutants are warranted to define the sequence polymorphisms responsible for temperature sensitivity.

The Neurospora crassa cyt-20 gene encodes cytosolic and mitochondrial valyl-tRNA synthetases and may have a second function in addition to protein synthesis

1991 ◽  
Vol 11 (8) ◽  
pp. 4022-4035
Author(s):  
A R Kubelik ◽  
B Turcq ◽  
A M Lambowitz
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Neurospora Crassa ◽  
Temperature Sensitivity ◽  
Temperature Sensitive ◽  
Cellular Transport ◽  
Missense Mutations ◽  
Reading Frame ◽  
Trna Synthetases ◽  
Cytosolic Protein

The cyt-20-1 mutant of Neurospora crassa is a temperature-sensitive, cytochrome b- and aa3-deficient strain that is severely deficient in both mitochondrial and cytosolic protein synthesis (R.A. Collins, H. Bertrand, R.J. LaPolla, and A.M. Lambowitz, Mol. Gen. Genet. 177:73-84, 1979). We cloned the cyt-20+ gene by complementation of the cyt-20-1 mutation and found that it contains a 1,093-amino-acid open reading frame (ORF) that encodes both the cytosolic and mitochondrial valyl-tRNA synthetases (vaIRSs). A second mutation, un-3, which is allelic with cyt-20-1, also results in temperature-sensitive growth, but not in gross deficiencies in cytochromes b and aa3 or protein synthesis. The un-3 mutant had also been reported to have pleiotropic defects in cellular transport process, resulting in resistance to amino acid analogs (M.S. Kappy and R.L. Metzenberg, J. Bacteriol. 94:1629-1637, 1967), but this resistance phenotype is separable from the temperature sensitivity in crosses and may result from a mutation in a different gene. The 1,093-amino-acid ORF encoding vaIRSs is the site of missense mutations resulting in temperature sensitivity in both cyt-20-1 and un-3 and is required for the transformation of both mutants. The opposite strand of the cyt-20 gene encodes an overlapping ORF of 532 amino acids, which may also be functional but is not required for transformation of either mutant. The cyt-20-1 mutation in the vaIRS ORF results in severe deficiencies of both mitochondrial and cytosolic vaIRS activities, whereas the un-3 mutation does not appear to result in a deficiency of these activities or of mitochondrial or cytosolic protein synthesis sufficient to account for its temperature-sensitive growth. The phenotype of the un-3 mutant raises the possibility that the vaIRS ORF has a second function in addition to protein synthesis.

scholarly journals Soil organic carbon stabilization mechanisms and temperature sensitivity in old terraced soils

2021 ◽  
Vol 18 (23) ◽  
pp. 6301-6312
Author(s):  
Pengzhi Zhao ◽  
Daniel Joseph Fallu ◽  
Sara Cucchiaro ◽  
Paolo Tarolli ◽  
Clive Waddington ◽  
...  
Keyword(s):  
Organic Carbon ◽  
Soil Organic Carbon ◽  
Temperature Sensitivity ◽  
Land Surface ◽  
C:N Ratio ◽  
Temperature Sensitive ◽  
Organic C ◽  
Fraction Composition ◽  
Soil Burial ◽  
C Cycle

Abstract. Being the most common human-created landforms, terrace construction has resulted in an extensive perturbation of the land surface. However, our mechanistic understanding of soil organic carbon (SOC) (de-)stabilization mechanisms and the persistence of SOC stored in terraced soils is far from complete. Here we explored the factors controlling SOC stability and the temperature sensitivity (Q10) of abandoned prehistoric agricultural terrace soils in NE England using soil fractionation and temperature-sensitive incubation combined with terrace soil burial-age measurements. Results showed that although buried terrace soils contained 1.7 times more unprotected SOC (i.e., coarse particulate organic carbon) than non-terraced soils at comparable soil depths, a significantly lower potential soil respiration was observed relative to a control (non-terraced) profile. This suggests that the burial of former topsoil due to terracing provided a mechanism for stabilizing SOC. Furthermore, we observed a shift in SOC fraction composition from particulate organic C towards mineral-protected C with increasing burial age. This clear shift to more processed recalcitrant SOC with soil burial age also contributes to SOC stability in terraced soils. Temperature sensitivity incubations revealed that the dominant controls on Q10 depend on the terrace soil burial age. At relatively younger ages of soil burial, the reduction in substrate availability due to SOC mineral protection with aging attenuates the intrinsic Q10 of SOC decomposition. However, as terrace soil becomes older, SOC stocks in deep buried horizons are characterized by a higher temperature sensitivity, potentially resulting from the poor SOC quality (i.e., soil C:N ratio). In conclusion, terracing in our study site has stabilized SOC as a result of soil burial during terrace construction. The depth–age patterns of Q10 and SOC fraction composition of terraced soils observed in our study site differ from those seen in non-terraced soils, and this has implications when assessing the effects of climate warming and terrace abandonment on the terrestrial C cycle.

Temperature Sensitivity of Intracellular and Extracellular Soil Enzyme Activities

2021 ◽  
Author(s):  
Adetunji Alex Adekanmbi ◽  
Laurence Dale ◽  
Liz Shaw ◽  
Tom Sizmur
Keyword(s):  
Enzyme Activity ◽  
Soil Temperature ◽  
Temperature Sensitivity ◽  
Extracellular Enzymes ◽  
Extracellular Enzyme ◽  
Daily Maximum ◽  
Temperature Sensitive ◽  
Intracellular Enzyme ◽  
Temperature Changes ◽  
Som Decomposition

<p>Predicting the pattern of soil organic matter (SOM) decomposition as a feedback to climate change, via release of CO<sub>2</sub>, is extremely complex and has received much attention. However, investigations often do not differentiate between the extracellular and intracellular processes involved and work is needed to identify their relative temperature sensitivities. Samples were collected from a grassland soil at Sonning, UK with average daily maximum and minimum soil temperature of 15 °C and 5 °C. We measured potential activities of β-glucosidase (BG) and chitinase (NAG) (extracellular enzymes) and glucose-induced CO<sub>2 </sub>respiration (intracellular enzymes) at a range of assay temperatures (5 °C, 15 °C, 26 °C, 37<sup>  </sup>°C, and 45 °C). The temperature coefficient Q<sub>10</sub> (the increase in enzyme activity that occurs after a 10 °C increase in soil temperature) was calculated to assess the temperature sensitivity of intracellular and extracellular enzymes activities. Between 5 °C and 15 °C intracellular and extracellular enzyme activities had equal temperature sensitivity, but between 15 °C and 26°C intracellular enzyme activity was more temperature sensitive than extracellular enzyme activity and between 26 °C and 37 °C extracellular enzyme activity was more temperature sensitive than intracellular enzyme activity. This result implies that extracellular depolymerisation of higher molecular weight organic compounds is more sensitive to temperature changes at higher temperatures (e.g. changes to daily maximum summer temperature) but the intracellular respiration of the generated monomers is more sensitive to temperature changes at moderate temperatures (e.g. changes to daily mean summer temperature). We therefore conclude that the extracellular and intracellular steps of SOM mineralisation are not equally sensitive to changes in soil temperature. The finding is important because we have observed greater increases in average daily minimum temperatures than average daily mean or maximum temperatures due to increased cloud cover and sulphate aerosol emission. Accounting for this asymmetrical global warming may reduce the importance of extracellular depolymerisation and increase the importance of intracellular catalytic activities as the rate limiting step of SOM decomposition.</p>

scholarly journals Environmental and biological controls on Na∕Ca ratios in scleractinian cold-water corals

2019 ◽  
Vol 16 (18) ◽  
pp. 3565-3582 ◽  
Author(s):  
Nicolai Schleinkofer ◽  
Jacek Raddatz ◽  
André Freiwald ◽  
David Evans ◽  
Lydia Beuck ◽  
...  
Keyword(s):  
Temperature Sensitivity ◽  
Inductively Coupled Plasma ◽  
Cold Water ◽  
Inverse Correlation ◽  
Optical Emission ◽  
Emission Spectrometry ◽  
Temperature Sensitive ◽  
Lophelia Pertusa ◽  
Inductively Coupled ◽  
The Impact

Abstract. Here we present a comprehensive attempt to correlate aragonitic Na∕Ca ratios from Desmophyllum pertusum (formerly known as Lophelia pertusa), Madrepora oculata and a caryophylliid cold-water coral (CWC) species with different seawater parameters such as temperature, salinity and pH. Living CWC specimens were collected from 16 different locations and analyzed for their Na∕Ca ratios using solution-based inductively coupled plasma-optical emission spectrometry (ICP-OES) measurements. The results reveal no apparent correlation with salinity (30.1–40.57 g kg−1) but a significant inverse correlation with temperature (-0.31±0.04 mmolmol-1∘C-1). Other marine aragonitic organisms such as Mytilus edulis (inner aragonitic shell portion) and Porites sp. exhibit similar results highlighting the consistency of the calculated CWC regressions. Corresponding Na∕Mg ratios show a similar temperature sensitivity to Na∕Ca ratios, but the combination of two ratios appears to reduce the impact of vital effects and domain-dependent geochemical variation. The high degree of scatter and elemental heterogeneities between the different skeletal features in both Na∕Ca and Na∕Mg, however, limit the use of these ratios as a proxy and/or make a high number of samples necessary. Additionally, we explore two models to explain the observed temperature sensitivity of Na∕Ca ratios for an open and semi-enclosed calcifying space based on temperature-sensitive Na- and Ca-pumping enzymes and transport proteins that change the composition of the calcifying fluid and consequently the skeletal Na∕Ca ratio.

Temperature-dependent skeletal muscle dysfunction in rats with congestive heart failure

2005 ◽  
Vol 99 (4) ◽  
pp. 1500-1507 ◽  
Author(s):  
H.-M. Schiøtz Thorud ◽  
E. Verburg ◽  
P. K. Lunde ◽  
T. A. Strømme ◽  
I. Sjaastad ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Temperature Sensitivity ◽  
Muscle Dysfunction ◽  
Temperature Sensitive ◽  
Relaxation Rates ◽  
Intracellular Ca ◽  
Slow Twitch Muscle ◽  
Slow Twitch ◽  
The Difference ◽  
Contraction And Relaxation

Abnormalities in the excitation-contraction coupling of slow-twitch muscle seem to explain the slowing and increased fatigue observed in congestive heart failure (CHF). However, it is not known which elements of the excitation-contraction coupling might be affected. We hypothesize that the temperature sensitivity of contractile properties of the soleus muscle might be altered in CHF possibly because of alterations of the temperature sensitivity of intracellular Ca2+ handling. We electrically stimulated the in situ soleus muscle of anesthetised rats that had 6-wk postinfarction CHF using 1 and 50 Hz and using a fatigue protocol (5-Hz stimulation for 30 min) at 35, 37, and 40°C. Ca2+ uptake and release were measured in sarcoplasmic reticulum vesicles at various temperatures. Contraction and relaxation rates of the soleus muscle were slower in CHF than in sham at 35°C, but the difference was almost absent at 40°C. The fatigue protocol revealed that force development was more temperature sensitive in CHF, whereas contraction and relaxation rates were less temperature sensitive in CHF than in sham. The Ca2+ uptake and release rates did not correlate to the difference between CHF and sham regarding contractile properties or temperature sensitivity. In conclusion, the discrepant results regarding altered temperature sensitivity of contraction and relaxation rates in the soleus muscle of CHF rats compared with Ca2+ release and uptake rates in vesicles indicate that the molecular cause of slow-twitch muscle dysfunction in CHF is not linked to the intracellular Ca2+ cycling.

Linking temperature sensitivities of soil enzymes to temperature responses of different organic matter pools in the DAISY model

2020 ◽  
Author(s):  
Moritz Laub ◽  
Rana Shahbaz Ali ◽  
Michael Scott Demyan ◽  
Yvonne Funkuin Nkwain ◽  
Christian Poll ◽  
...  
Keyword(s):  
Temperature Sensitivity ◽  
Soil Enzymes ◽  
Field Experiments ◽  
Bare Soil ◽  
Temperature Sensitive ◽  
Model Errors ◽  
Temperature Range ◽  
Soil Microbial ◽  
Bare Fallow ◽  
The Individual

<p>Soil organic carbon (SOC) losses under a changing climate are driven by the temperature sensitivity of SOC mineralization (usually expressed as Q<sub>10</sub>, the multiplier of activity with 10 °C temperature increase). The activation energy theory (AET) suggests that, due to higher activation energies, the more complex the carbon, the higher is mineralization Q<sub>10</sub>. However, studies on Q<sub>10 </sub>have been inconsistent with regard to AET. Measurements of potential soil enzymes activity Q<sub>10 </sub>even contradicted AET: Phenoloxidase (representing complex carbon) had consistently lower Q<sub>10 </sub>than the more labile xylanase and glucosidase. This study used two approaches of examining Q<sub>10</sub> in SOC modeling: 1) Bayesian calibration (BC) and 2) using different measured enzyme Q<sub>10</sub> as proxies for mineralization Q<sub>10 </sub>of different SOC pools. The SOC model was DAISY (S. Hansen et al., 2012). BC informed Q<sub>10</sub> by field measured data, while the second approach tested if directly using enzyme Q<sub>10 </sub>(of phenoloxidase, glucosidase and xylanase) for DAISY pools improved simulation results. Both approaches used the temperature sensitive measurements of CO<sub>2</sub> evolution and soil microbial biomass. The measured enzyme Q<sub>10</sub> were from field manipulation experiments with bare fallow and vegetated plots in the two regions of Kraichgau and Swabian Jura in Southwest Germany. The enzyme-derived Q<sub>10</sub> were used for modelling those fields and furthermore for in‑situ litterbag decomposition experiments at 20 sites in the same region. Two further laboratory experiments with temperature manipulation were included: an incubation of the field residues into soil and an incubation of bare soil from the start and year 50 of a long duration bare fallow (from Ultuna). The BC made use of CO<sub>2</sub> and microbial data to inform about the range of Q<sub>10</sub> of different carbon pools for the individual experiments and combined data.</p><p>The BC of the residue incubation experiment constrained Q<sub>10</sub> for metabolic (~3) and structural litter (~2). Estimated 95% credibility intervals did not overlap. The BC for Ultuna could constrain the slow and fast SOC pool with Q<sub>10</sub> ~2.8 and ~3, respectively, but credibility intervals of both pools overlapped. The Q<sub>10</sub> of field experiments, which had most abundant data, could not be constrained by BC, probably because their annual temparature variability was too low. However, the model errors of the field experiment could be reduced by the second approach, when the Q<sub>10 </sub>of phenoloxidase was used for to the structural litter pool as well as for the fast and slow SOC pools. Thus regional enzyme Q<sub>10</sub> improved the model fit but only for regional simulations. Therefore, they could be useful proxies when natural temperature range is too small to inform temperature sensitivity by BC. Any trends found in this study contradicted AET, both from measured enzymes and BC of the incubation experiments. This calls for alternative Q<sub>10</sub> hypotheses and the need for individual Q<sub>10</sub> values for different SOC pool rather than a general one. BC approaches would benefit from a wider temperature range of field experiments and understanding what causes variable enzyme Q<sub>10</sub> could help to improve future SOC models.</p>

scholarly journals The Yeast Nα-Acetyltransferase NatA Is Quantitatively Anchored to the Ribosome and Interacts with Nascent Polypeptides

2003 ◽  
Vol 23 (20) ◽  
pp. 7403-7414 ◽  
Author(s):  
Matthias Gautschi ◽  
Sören Just ◽  
Andrej Mun ◽  
Suzanne Ross ◽  
Peter Rücknagel ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Mating Type ◽  
Temperature Sensitivity ◽  
Temperature Sensitive ◽  
Wide Range ◽  
Close Proximity ◽  
N Terminus ◽  
Catalytically Active ◽  
Covalently Linked ◽  
Silent Mating Type Loci

ABSTRACT The majority of cytosolic proteins in eukaryotes contain a covalently linked acetyl moiety at their very N terminus. The mechanism by which the acetyl moiety is efficiently transferred to a large variety of nascent polypeptides is currently only poorly understood. Yeast Nα -acetyltransferase NatA, consisting of the known subunits Nat1p and the catalytically active Ard1p, recognizes a wide range of sequences and is thought to act cotranslationally. We found that NatA was quantitatively bound to ribosomes via Nat1p and contained a previously unrecognized third subunit, the Nα -acetyltransferase homologue Nat5p. Nat1p not only anchored Ard1p and Nat5p to the ribosome but also was in close proximity to nascent polypeptides, independent of whether they were substrates for Nα -acetylation or not. Besides Nat1p, NAC (nascent polypeptide-associated complex) and the Hsp70 homologue Ssb1/2p interact with a variety of nascent polypeptides on the yeast ribosome. A direct comparison revealed that Nat1p required longer nascent polypeptides for interaction than NAC and Ssb1/2p. Δnat1 or Δard1 deletion strains were temperature sensitive and showed derepression of silent mating type loci while Δnat5 did not display any obvious phenotype. Temperature sensitivity and derepression of silent mating type loci caused by Δnat1 or Δard1 were partially suppressed by overexpression of SSB1. The combination of data suggests that Nat1p presents the N termini of nascent polypeptides for acetylation and might serve additional roles during protein synthesis.

scholarly journals Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport.

1991 ◽  
Vol 114 (4) ◽  
pp. 671-679 ◽  
Author(s):  
T Oka ◽  
S Nishikawa ◽  
A Nakano
Keyword(s):  
Temperature Sensitivity ◽  
Protein Function ◽  
Secretory Pathway ◽  
Protein Transport ◽  
Temperature Sensitive ◽  
Transport Reaction ◽  
Golgi Transport ◽  
Gtp Binding

In the yeast secretory pathway, two genes SEC12 and SAR1, which encode a 70-kD integral membrane protein and a 21-kD GTP-binding protein, respectively, cooperate in protein transport from the ER to the Golgi apparatus. In vivo, the elevation of the SAR1 dosage suppresses temperature sensitivity of the sec12 mutant. In this paper, we show cell-free reconstitution of the ER-to-Golgi transport that depends on both of these gene products. First, the membranes from the sec12 mutant cells reproduce temperature sensitivity in the in vitro ER-to-Golgi transport reaction. Furthermore, the addition of the Sar1 protein completely suppresses this temperature-sensitive defect of the sec12 membranes. The analysis of Sar1p partially purified by E. coli expression suggests that GTP hydrolysis is essential for Sar1p to execute its function.

scholarly journals A TEMPERATURE-SENSITIVE MUTANT IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (1) ◽  
pp. 107-114
Author(s):  
J Wynne McCoy
Keyword(s):  
Mating Type ◽  
Temperature Sensitivity ◽  
Tetrahymena Pyriformis ◽  
Recessive Allele ◽  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Interstrain Differences ◽  
Show Evidence ◽  
The Cross

ABSTRACT After treatment with nitrosoguanidine a mutation to temperature sensitivity was obtained in Tetrahymena pyriformis, syngen 1. The trait is controlled by a recessive allele, ts, at a locus linked to serotype locus T. IS is completely recessive, unlike any other allele studied in this organism, and the heterozygotes do not show vegetative assortment. The cross which revealed the linkage of ts and T failed to show evidence of the linkage of mt (mating type) and E-1 (esterase-I) which has been demonstrated in other crosses (ALLEN 1964; DOERDER 1972), but revealed a third case of linkage, involving mt and TO (tetrazolium oxidase). Taken together, these results are presumptive evidence for large interstrain differences in recombination properties within syngen 1.

Sign in / Sign up

Export Citation Format

Share Document