Apr 26, 2024
New research on the body's liver response explains why we're triggered by food. Click to read the full fact.
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New research on the body's liver response explains why we're triggered by food. Click to read the full fact.
when i took bio i meant human physiology not some non-cyclic photophosphorylation shit😭😭😭😭😭😭😭😭
Features of Films
Living in a tight-knit community can provide safety and support. Bacteria find this too, and huddle together to form dense biofilms, which increase their survival and infectious potency. These films are glued together by a sugary slime called exopolysaccharides, without which the structure begins to fall apart. A new study has revealed a key factor in the production of this material in cholera biofilms (Vibrio exopolysaccharide, VPS). By adjusting the amount to which a particular enzyme attaches to and removes phosphate (dephosphorylation), the researchers changed the structural integrity of the biofilms (pictured, in several experiments). The production of VPS was directly regulated by the phosphorylation status, revealing a potential weakness that treatments could target to help prevent cholera settling in. Furthermore, these systems are similar among many bacteria that produce equivalent biofilms, meaning the insights could help tackle a wide range of diseases.
Written by Anthony Lewis
Image from work by Carmen Schwechheimer and colleagues
University of California—Santa Cruz, Santa Cruz, CA, USA
Image originally published with a Creative Commons Attribution 4.0 International (CC BY 4.0)
Published in PLOS Pathogens, August 2020
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After reading Dan Urry’s work on what he calls the apolar-polar repulsive free energy of hydration, I am less puzzled by biology’s obsession with phosphorylating and dephosphorylating proteins.
Basically, due to the competition between hydrophilic and hydrophobic surfaces for hydration, the extremely hydrophilic phosphate causes nearby hydrophobically associated regions to dissociate. Contrariwise, removing a phosphate group encourages nearby hydrophobic regions to associate (i.e. stick together). (This only makes sense in light of the fact that hydrophobic hydration is enthalpically favorable but entropically unfavorable.)
So (de)phosphorylating a protein at the right site can selectively, reversibly, and locally add or subtract stickiness, causing a conformational change.
Abstract Protein kinases represent one of the largest eukaryotic enzyme superfamilies. However, only a few can directly phosphorylate tubuli
Abstract Protein kinases represent one of the largest eukaryotic enzyme superfamilies. However, only a few can directly phosphorylate tubulin and contribute to the modulation of the “tubulin code.” The authors previously confirmed the structural and functional homology of the plant protein kinase IREH1 and members of the mammalian MAST kinase family. Their participation in the regulation of the microtubule system in plant and animal cells was also experimentally confirmed. At the same time, the direct contribution of MAST/IRE to the “tubulin code” remains unclear. In the current study, based on bioinformatical and structural biology methods, the possibility of such an interaction was evaluated. The target sites of MAST/IRE-phosphorylation of tubulin were predicted based on similarity to the generalized specific profiles. Two potential MAST/IRE specific sites, conserved in human and Arabidopsis tubulins were selected: Thr73 (80) exists in most isotypes of α-tubulin and Ser115 was found in the majority of human and plant isotypes of β-tubulin. It was predicted that phosphorylation of the first site can affect the assembly of α/β-tubulin heterodimer, and phosphorylation of the second may affect the interaction between neighboring protofilaments of microtubules. The last site Ser433, was found in both γ-tubulin isotypes of A. thaliana, but it was absent in mammals. The external position of Ser433 in plant γ-tubulin allows for suggesting that phosphorylation of this amino acid can affect the structure of the γTuRC complex but it does not affect inner contacts of γTuSC and their interaction in the ring.
Phosphorylation:Metabolic Pathway
Phosphorylation: The Powerhouse of Cellular Energy In the bustling world of cells, energy is the driving force behind every process, from building proteins to transporting nutrients. And one of the most crucial players in this energy-generating game is phosphorylation. What is Phosphorylation? Phosphorylation is the process of adding a phosphate group (PO43-) to a molecule. This process can…
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The factors that determine these changes are not completely understood, but changes in the phosphorylation state of PINs mediated by the kinase PINOID and the phosphatase PP2 can have significant effects on PIN localization.
"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.
The phosphorylation-activated response regulators, many of which function as transcription factors, then bring about the cellular response.
"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.