scholarly journals Acidic Region

2020 ◽  
Author(s):  
Keyword(s):  
Acidic Region

scholarly journals Overexpression of SIS2, which contains an extremely acidic region, increases the expression of SWI4, CLN1 and CLN2 in sit4 mutants.

Genetics ◽  
1995 ◽  
Vol 139 (1) ◽  
pp. 95-107 ◽  
Author(s):  
C J Di Como ◽  
R Bose ◽  
K T Arndt
Keyword(s):  
Growth Rate ◽  
Protein Phosphatase ◽  
Rnase A ◽  
Micrococcal Nuclease ◽  
Nuclear Fraction ◽  
High Copy Number Plasmid ◽  
Carboxyl Terminal ◽  
Rna Accumulation ◽  
Bud Initiation ◽  
Acidic Region

Abstract The Saccharomyces cerevisiae SIS2 gene was identified by its ability, when present on a high copy number plasmid, to increase dramatically the growth rate of sit4 mutants. SIT4 encodes a type 2A-related protein phosphatase that is required in late G1 for normal G1 cyclin expression and for bud initiation. Overexpression of SIS2, which contains an extremely acidic carboxyl terminal region, stimulated the rate of CLN1, CLN2, SWI4 and CLB5 expression in sit4 mutants. Also, overexpression of SIS2 in a CLN1 cln2 cln3 strain stimulated the growth rate and the rate of CLN1 and CLB5 RNA accumulation during late G1. The SIS2 protein fractionated with nuclei and was released from the nuclear fraction by treatment with either DNase I or micrococcal nuclease, but not by RNase A. This result, combined with the finding that overexpression of SIS2 is extremely to a strain containing lower than normal levels of histones H2A and H2B, suggests that SIS2 might function to stimulate transcription via an interaction with chromatin.

Acidic Region Residues 1680–1684 in the A3 Domain of Factor VIII Contain a Thrombin-Interactive Site Responsible for Proteolytic Cleavage at Arg1689

2021 ◽  
Author(s):  
Yuto Nakajima ◽  
Hiroaki Minami ◽  
Keiji Nogami
Keyword(s):  
Surface Plasmon Resonance ◽  
Factor Viii ◽  
Heavy Chain ◽  
Synthetic Peptides ◽  
C2 Domain ◽  
Wild Type ◽  
Cross Link ◽  
Domain Specific ◽  
Cofactor Activity ◽  
Acidic Region

AbstractFactor VIII (FVIII) is activated by thrombin-catalyzed cleavage at Arg372, Arg740, and Arg1689. Our previous studies suggested that thrombin interacted with the FVIII C2 domain specific for cleavage at Arg1689. An alternative report demonstrated, however, that a recombinant (r)FVIII mutant lacking the C2 domain retained >50% cofactor activity, indicating the presence of other thrombin-interactive site(s) associated with cleavage at Arg1689. We have focused, therefore, on the A3 acidic region of FVIII, similar to the hirugen sequence specific for thrombin interaction (54–65 residues). Two synthetic peptides, spanning residues 1659–1669 with sulfated Tyr1664 and residues 1675–1685 with sulfated Try1680, inhibited thrombin-catalyzed FVIII activation and cleavage at Arg1689. Treatment with 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide to cross-link thrombin with either peptide showed possible contributions of both 1664–1666 and 1683–1684 residues for thrombin interaction. Thrombin-catalyzed activation and cleavage at Arg1689 in the alanine-substituted rFVIII mutants within 1663–1666 residues were similar to those of wild type (WT). Similar studies of 1680–1684 residues, however, demonstrated that activation and cleavage by thrombin of the FVIII mutant with Y1680A or D1683A/E1684A, in particular, were severely or moderately reduced to 20 to 30% or 60 to 70% of WT, respectively. Surface plasmon resonance-based analysis revealed that thrombin interacted with both Y1680A and D1683A/E1684A mutants with approximately sixfold weaker affinities of WT. Cleavage at Arg1689 in the isolated light-chain fragments from both mutants was similarly depressed, independently of the heavy-chain subunit. In conclusion, the 1680–1684 residues containing sulfated Tyr1680 in the A3 acidic region also contribute to a thrombin-interactive site responsible for FVIII activation through cleavage at Arg1689.

scholarly journals Enhancement of mDia2 activity by Rho-kinase-dependent phosphorylation of the diaphanous autoregulatory domain

2011 ◽  
Vol 439 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Dean P. Staus ◽  
Joan M. Taylor ◽  
Christopher P. Mack
Keyword(s):  
Smooth Muscle ◽  
Actin Polymerization ◽  
Serum Response Factor ◽  
Rho Kinase ◽  
Specific Gene ◽  
Related Transcription Factor ◽  
Inhibitory Domain ◽  
Serum Response ◽  
Acidic Region ◽  
Basic Region

It is clear that RhoA activates the DRF (diaphanous-related formin) mDia2 by disrupting the molecular interaction between the DAD (diaphanous autoregulatory domain) and the DID (diaphanous inhibitory domain). Previous studies indicate that a basic motif within the DAD contributes to mDia2 auto-inhibition, and results shown in the present study suggest these residues bind a conserved acidic region within the DID. Furthermore, we demonstrate that mDia2 is phosphorylated by ROCK (Rho-kinase) at two conserved residues (Thr1061 and Ser1070) just C-terminal to the DAD basic region. Phosphomimetic mutations to these residues in the context of the full-length molecule enhanced mDia2 activity as measured by increased actin polymerization, SRF (serum response factor)-dependent smooth muscle-specific gene transcription, and nuclear localization of myocardin-related transcription factor B. Biochemical and functional data indicate that the T1061E/S1070E mutation significantly inhibited the ability of DAD to interact with DID and enhanced mDia2 activation by RhoA. Taken together, the results of the present study indicate that ROCK-dependent phosphorylation of the mDia2 DAD is an important determinant of mDia2 activity and that this signalling mechanism affects actin polymerization and smooth muscle cell-specific gene expression.

Spinalin, a new glycine- and histidine-rich protein in spines of Hydra nematocysts

1998 ◽  
Vol 111 (11) ◽  
pp. 1545-1554 ◽  
Author(s):  
A.W. Koch ◽  
T.W. Holstein ◽  
C. Mala ◽  
E. Kurz ◽  
J. Engel ◽  
...  
Keyword(s):  
External Surface ◽  
Insoluble Fraction ◽  
Cdna Clones ◽  
Mature Protein ◽  
Capsule Wall ◽  
The Matrix ◽  
Acidic Region ◽  
Basic Region ◽  
Full Length Clone

Here we present the cloning, expression and immunocytochemical localization of a novel 24 kDa protein, designated spinalin, which is present in the spines and operculum of Hydra nematocysts. Spinalin cDNA clones were identified by in situ hybridization to differentiating nematocytes. Sequencing of a full-length clone revealed the presence of an N-terminal signal peptide, suggesting that the mature protein is sorted via the endoplasmic reticulum to the post-Golgi vacuole in which the nematocyst is formed. The N-terminal region of spinalin (154 residues) is very rich in glycines (48 residues) and histidines (33 residues). A central region of 35 residues contains 19 glycines, occurring mainly as pairs. For both regions a polyglycine-like structure is likely and this may be stabilized by hydrogen bond-mediated chain association. Similar sequences found in loricrins, cytokeratins and avian keratins are postulated to participate in formation of supramolecular structures. Spinalin is terminated by a basic region (6 lysines out of 15 residues) and an acidic region (9 glutamates and 9 aspartates out of 32 residues). Western blot analysis with a polyclonal antibody generated against a recombinant 19 kDa fragment of spinalin showed that spinalin is localized in nematocysts. Following dissociation of the nematocyst's capsule wall with DTT, spinalin was found in the insoluble fraction containing spines and the operculum. Immunocytochemical analysis of developing nematocysts revealed that spinalin first appears in the matrix but then is transferred through the capsule wall at the end of morphogenesis to form spines on the external surface of the inverted tubule and the operculum.

scholarly journals Human traces in the bryophyte flora of the summit region of Karkonosze Mts (Polish side)

2011 ◽  
Vol 76 (4) ◽  
pp. 345-349 ◽  
Author(s):  
Ewa Fudali
Keyword(s):  
Building Material ◽  
Ecological Preferences ◽  
Summit Region ◽  
Acidic Region

Based on results of the bryofloristic investigations carried out in 2006 along tourist roads and around mountain chalets the problem of bryophyte response to the tourist utilization of the summit region of Karkonosze Mts is discussed here. The hypothesis that introduction of cement as building material might have caused the income and spread of subneutral or basiphilous ruderal species in that naturally acidic region was formulated and tested. In result 45 species were found, of which the majority do not occur in natural sites in the Karkonosze Mts. Among them 20 species are convinced to be highly hemerophilous. Most of the found species were eurytopic, only 14 prefered subneutral or basic substrata. Many of them produced sporogonia, what indicates high reproduction potential. It seems that the phenomenon of synanthropisation is limited mainly to places in which cement (as mortar or concrete) has been used. The list of bryophytes found around all the anthropogenic sites and along the tourist roads in the summit region of Polish part of the massif with brief characteristics of their ecological preferences has been included.

scholarly journals The Acidic Region and Conserved Putative Protein Kinase C Phosphorylation Site in Nef Are Important for SIV Replication in Rhesus Macaques

Virology ◽  
1999 ◽  
Vol 257 (1) ◽  
pp. 138-155 ◽  
Author(s):  
Silke Carl ◽  
A.John Iafrate ◽  
Sabine M. Lang ◽  
Christiane Stahl-Hennig ◽  
Eva M. Kuhn ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rhesus Macaques ◽  
Phosphorylation Site ◽  
Putative Protein ◽  
Kinase C ◽  
Acidic Region ◽  
Putative Protein Kinase

scholarly journals A repetitive acidic region contributes to the extremely rapid degradation of the cell-context essential protein TRIM52

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Kathrin Hacker ◽  
Stefan Benke ◽  
Benedikt Agerer ◽  
Sara Scinicariello ◽  
Valentina Budroni ◽  
...  
Keyword(s):  
Rapid Degradation ◽  
Essential Protein ◽  
Acidic Region

scholarly journals OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Kangxi Du ◽  
Qiang Luo ◽  
Liufan Yin ◽  
Jiabing Wu ◽  
Yuhao Liu ◽  
...  
Keyword(s):  
Nucleosome Occupancy ◽  
Functional Characterization ◽  
Histone Chaperone ◽  
Recognition Mechanism ◽  
Developmental Defects ◽  
Dynamic Regulation ◽  
Genome Wide ◽  
Domain Protein ◽  
Acidic Region

Abstract While the yeast Chz1 acts as a specific histone-chaperone for H2A.Z, functions of CHZ-domain proteins in multicellular eukaryotes remain obscure. Here, we report on the functional characterization of OsChz1, a sole CHZ-domain protein identified in rice. OsChz1 interacts with both the canonical H2A-H2B dimer and the variant H2A.Z-H2B dimer. Within crystal structure the C-terminal region of OsChz1 binds H2A-H2B via an acidic region, pointing to a previously unknown recognition mechanism. Knockout of OsChz1 leads to multiple plant developmental defects. At genome-wide level, loss of OsChz1 causes mis-regulations of thousands of genes and broad alterations of nucleosome occupancy as well as reductions of H2A.Z-enrichment. While OsChz1 associates with chromatin regions enriched of repressive histone marks (H3K27me3 and H3K4me2), its loss does not affect the genome landscape of DNA methylation. Taken together, it is emerging that OsChz1 functions as an important H2A/H2A.Z-H2B chaperone in dynamic regulation of chromatin for higher eukaryote development.

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