scholarly journals Molecular basis of UHRF1 allosteric activation for synergistic histone modification binding by PI5P

2021 ◽  
Author(s):  
Papita Mandal ◽  
Zhadyra Yerkesh ◽  
Vladlena Kharchenko ◽  
Levani Zandarashvili ◽  
Dalila Bensaddek ◽  
...  
Keyword(s):  
Histone Modification ◽  
Molecular Basis ◽  
Allosteric Regulation ◽  
Head Group ◽  
Polar Head Group ◽  
Molecular Function ◽  
Multidomain Proteins ◽  
Allosteric Activation ◽  
Polar Head ◽  
Conformational Rearrangements

Chromatin marks are recognized by distinct binding modules many of which are embedded in multidomain proteins or complexes. How the different protein functionalities of complex chromatin modulators are regulated is often unclear. Using a combination of biochemical, biophysical and structural approaches we delineated the regulation of the H3unmodified and H3K9me binding activities of the multidomain UHRF1 protein. The phosphoinositide PI5P interacts with two distant flexible linker regions of UHRF1 in a mode that is dependent on the polar head group and the acyl part of the phospholipid. The associated conformational rearrangements stably position the H3unmodified and H3K9me3 histone recognition modules of UHRF1 for multivalent and synergistic binding of the H3 tail. Our work highlights a novel molecular function for PI5P outside of the context of lipid mono- or bilayers and establishes a molecular paradigm for the allosteric regulation of complex, multidomain chromatin modulators by small cellular molecules.

The effect of polar head group of dodecyl surfactants on the growth of wheat and cucumber

Chemosphere ◽  
2020 ◽  
Vol 254 ◽  
pp. 126918
Author(s):  
Aleksandar Tot ◽  
Ivana Maksimović ◽  
Marina Putnik-Delić ◽  
Milena Daničić ◽  
Slobodan Gadžurić ◽  
...  
Keyword(s):  
Head Group ◽  
Polar Head Group ◽  
Polar Head

Glycosylinositol phosphoceramide-specific phospholipase D activity catalyzes transphosphatidylation

2019 ◽  
Vol 166 (5) ◽  
pp. 441-448 ◽  
Author(s):  
Rumana Yesmin Hasi ◽  
Makoto Miyagi ◽  
Katsuya Morito ◽  
Toshiki Ishikawa ◽  
Maki Kawai-Yamada ◽  
...  
Keyword(s):  
Chain Length ◽  
Phospholipase D ◽  
Secondary Alcohol ◽  
Primary Alcohol ◽  
Tertiary Alcohol ◽  
Head Group ◽  
Polar Head Group ◽  
Polar Head ◽  
A Chain ◽  
Sugar Chains

Abstract Glycosylinositol phosphoceramide (GIPC) is the most abundant sphingolipid in plants and fungi. Recently, we detected GIPC-specific phospholipase D (GIPC-PLD) activity in plants. Here, we found that GIPC-PLD activity in young cabbage leaves catalyzes transphosphatidylation. The available alcohol for this reaction is a primary alcohol with a chain length below C4. Neither secondary alcohol, tertiary alcohol, choline, serine nor glycerol serves as an acceptor for transphosphatidylation of GIPC-PLD. We also found that cabbage GIPC-PLD prefers GIPC containing two sugars. Neither inositol phosphoceramide, mannosylinositol phosphoceramide nor GIPC with three sugar chains served as substrate. GIPC-PLD will become a useful catalyst for modification of polar head group of sphingophospholipid.

Changes in phospholipid polar head group turnover in SV40-transformed hamster fibroblasts

FEBS Letters ◽  
1982 ◽  
Vol 139 (2) ◽  
pp. 217-220 ◽  
Author(s):  
Cécile Maziére ◽  
Jean-Claude Maziére ◽  
Liliana Mora ◽  
Jacques Polonovski
Keyword(s):  
Head Group ◽  
Polar Head Group ◽  
Polar Head

scholarly journals Biosynthesis of Ether-Type Polar Lipids in Archaea and Evolutionary Considerations

2007 ◽  
Vol 71 (1) ◽  
pp. 97-120 ◽  
Author(s):  
Yosuke Koga ◽  
Hiroyuki Morii
Keyword(s):  
Mevalonate Pathway ◽  
Polar Lipids ◽  
In Vivo Studies ◽  
Head Group ◽  
Polar Head Group ◽  
Phospholipid Synthesis ◽  
Polar Head ◽  
Head Groups

SUMMARY This review deals with the in vitro biosynthesis of the characteristics of polar lipids in archaea along with preceding in vivo studies. Isoprenoid chains are synthesized through the classical mevalonate pathway, as in eucarya, with minor modifications in some archaeal species. Most enzymes involved in the pathway have been identified enzymatically and/or genomically. Three of the relevant enzymes are found in enzyme families different from the known enzymes. The order of reactions in the phospholipid synthesis pathway (glycerophosphate backbone formation, linking of glycerophosphate with two radyl chains, activation by CDP, and attachment of common polar head groups) is analogous to that of bacteria. sn-Glycerol-1-phosphate dehydrogenase is responsible for the formation of the sn-glycerol-1-phosphate backbone of phospholipids in all archaea. After the formation of two ether bonds, CDP-archaeol acts as a common precursor of various archaeal phospholipid syntheses. Various phospholipid-synthesizing enzymes from archaea and bacteria belong to the same large CDP-alcohol phosphatidyltransferase family. In short, the first halves of the phospholipid synthesis pathways play a role in synthesis of the characteristic structures of archaeal and bacterial phospholipids, respectively. In the second halves of the pathways, the polar head group-attaching reactions and enzymes are homologous in both domains. These are regarded as revealing the hybrid nature of phospholipid biosynthesis. Precells proposed by Wächtershäuser are differentiated into archaea and bacteria by spontaneous segregation of enantiomeric phospholipid membranes (with sn-glycerol-1-phosphate and sn-glycerol-3-phosphate backbones) and the fusion and fission of precells. Considering the nature of the phospholipid synthesis pathways, we here propose that common phospholipid polar head groups were present in precells before the differentiation into archaea and bacteria.

Design, synthesis and evaluation of polar head group containing 2-keto-oxazole inhibitors of FAAH

2012 ◽  
Vol 20 (2) ◽  
pp. 1100-1112 ◽  
Author(s):  
Marion Rusch ◽  
Stefan Zahov ◽  
Ingrid R. Vetter ◽  
Matthias Lehr ◽  
Christian Hedberg
Keyword(s):  
Head Group ◽  
Polar Head Group ◽  
Design Synthesis ◽  
Polar Head
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