CARBOHYDRATE RECOGNITION AND SPECIFICITY DIFFERENCES OF BARLEY ALPHA-AMYLASE ISOZYMES: A NOVEL ROLE OF THEIR C-TERMINAL DOMAIN

2002 ◽  
Author(s):  
Xavier Robert ◽  
Richard Haser ◽  
Haruhide Mori ◽  
Birte Svensson ◽  
Nushin Aghajari
Keyword(s):  
Alpha Amylase ◽  
Carbohydrate Recognition ◽  
Terminal Domain

scholarly journals The role of the C-terminal domain in collagenase and stromelysin specificity.

1992 ◽  
Vol 267 (14) ◽  
pp. 9612-9618 ◽  
Author(s):  
G Murphy ◽  
J.A. Allan ◽  
F Willenbrock ◽  
M.I. Cockett ◽  
J.P. O'Connell ◽  
...  
Keyword(s):  
Terminal Domain

scholarly journals Catalytic effectiveness of human aldose reductase. Critical role of C-terminal domain.

1992 ◽  
Vol 267 (29) ◽  
pp. 20965-20970
Author(s):  
K.M. Bohren ◽  
C.E. Grimshaw ◽  
K.H. Gabbay
Keyword(s):  
Aldose Reductase ◽  
Critical Role ◽  
Terminal Domain

RNA secondary structure dependence in METTL3–METTL14 mRNA methylation is modulated by the N-terminal domain of METTL3

2020 ◽  
Vol 402 (1) ◽  
pp. 89-98
Author(s):  
Nathalie Meiser ◽  
Nicole Mench ◽  
Martin Hengesbach
Keyword(s):  
Secondary Structure ◽  
Rna Binding ◽  
Specific Protein ◽  
Structure Dependence ◽  
Terminal Domain ◽  
Methylation Assay ◽  
A Site ◽  
Methylation Activity

AbstractN6-methyladenosine (m6A) is the most abundant modification in mRNA. The core of the human N6-methyltransferase complex (MTC) is formed by a heterodimer consisting of METTL3 and METTL14, which specifically catalyzes m6A formation within an RRACH sequence context. Using recombinant proteins in a site-specific methylation assay that allows determination of quantitative methylation yields, our results show that this complex methylates its target RNAs not only sequence but also secondary structure dependent. Furthermore, we demonstrate the role of specific protein domains on both RNA binding and substrate turnover, focusing on postulated RNA binding elements. Our results show that one zinc finger motif within the complex is sufficient to bind RNA, however, both zinc fingers are required for methylation activity. We show that the N-terminal domain of METTL3 alters the secondary structure dependence of methylation yields. Our results demonstrate that a cooperative effect of all RNA-binding elements in the METTL3–METTL14 complex is required for efficient catalysis, and that binding of further proteins affecting the NTD of METTL3 may regulate substrate specificity.

scholarly journals Role of the N-terminal domain of the human DMC1 protein in octamer formation and DNA binding. VOLUME 280 (2005) PAGES 28382-28387

2006 ◽  
Vol 281 (50) ◽  
pp. 38966
Author(s):  
Takashi Kinebuchi ◽  
Wataru Kagawa ◽  
Hitoshi Kurumizaka ◽  
Shigeyuki Yokoyama
Keyword(s):  
Dna Binding ◽  
Terminal Domain

The Role of the N-Terminal Domain in the Regulation of the “Constitutively Active” Conformation of Protein Kinase CK2α: Insight from a Molecular Dynamics Investigation

ChemMedChem ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. 1207-1216 ◽  
Author(s):  
Andrea Cristiani ◽  
Giorgio Costa ◽  
Giorgio Cozza ◽  
Flavio Meggio ◽  
Leonardo Scapozza ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Protein Kinase ◽  
Active Conformation ◽  
Terminal Domain ◽  
Constitutively Active

scholarly journals Role of Amino-Terminal Domain in the Assembly Mechanism of Kainate-Subtype Glutamate Receptor Ion Channels

2014 ◽  
Vol 106 (2) ◽  
pp. 151a
Author(s):  
Sagar Chittori ◽  
Janesh Kumar ◽  
Suvendu Lomash ◽  
Huaying Zhao ◽  
Peter Schuck ◽  
...  
Keyword(s):  
Ion Channels ◽  
Glutamate Receptor ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Assembly Mechanism ◽  
Amino Terminal Domain

scholarly journals The Effect of Octapeptide Repeats on Prion Folding and Misfolding

2021 ◽  
Vol 22 (4) ◽  
pp. 1800
Author(s):  
Kun-Hua Yu ◽  
Mei-Yu Huang ◽  
Yi-Ru Lee ◽  
Yu-Kie Lin ◽  
Hau-Ren Chen ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Age Of Onset ◽  
Prion Diseases ◽  
Critical Role ◽  
Threshold Effect ◽  
Central Feature ◽  
Terminal Domain ◽  
Amyloid Aggregates

Misfolding of prion protein (PrP) into amyloid aggregates is the central feature of prion diseases. PrP has an amyloidogenic C-terminal domain with three α-helices and a flexible tail in the N-terminal domain in which multiple octapeptide repeats are present in most mammals. The role of the octapeptides in prion diseases has previously been underestimated because the octapeptides are not located in the amyloidogenic domain. Correlation between the number of octapeptide repeats and age of onset suggests the critical role of octapeptide repeats in prion diseases. In this study, we have investigated four PrP variants without any octapeptides and with 1, 5 and 8 octapeptide repeats. From the comparison of the protein structure and the thermal stability of these proteins, as well as the characterization of amyloids converted from these PrP variants, we found that octapeptide repeats affect both folding and misfolding of PrP creating amyloid fibrils with distinct structures. Deletion of octapeptides forms fewer twisted fibrils and weakens the cytotoxicity. Insertion of octapeptides enhances the formation of typical silk-like fibrils but it does not increase the cytotoxicity. There might be some threshold effect and increasing the number of peptides beyond a certain limit has no further effect on the cell viability, though the reasons are unclear at this stage. Overall, the results of this study elucidate the molecular mechanism of octapeptides at the onset of prion diseases.

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