Role of the C-Terminal Region of the B Component ofMethylosinus trichosporiumOB3b Methane Monooxygenase in the Regulation of Oxygen Activation†

Biochemistry ◽  
2006 ◽  
Vol 45 (5) ◽  
pp. 1459-1469 ◽  
Author(s):  
Jingyan Zhang ◽  
John D. Lipscomb
Keyword(s):  
Methane Monooxygenase ◽  
Oxygen Activation ◽  
Terminal Region

scholarly journals Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin

1991 ◽  
Vol 266 (23) ◽  
pp. 15334-15339 ◽  
Author(s):  
K. Palczewski ◽  
J. Buczyłko ◽  
N.R. Imami ◽  
J.H. McDowell ◽  
P.A. Hargrave
Keyword(s):  
Terminal Region ◽  
Carboxyl Terminal

scholarly journals Role of the amino-terminal region of the DnaA protein in opening of the duplex DNA at theoriCregion

1999 ◽  
Vol 176 (1) ◽  
pp. 163-167 ◽  
Author(s):  
Shinji Mima ◽  
Yoshihiro Yamagachi ◽  
Taemi Kondo ◽  
Tomofusa Tsuchiya ◽  
Tohru Mizushima
Keyword(s):  
Terminal Region ◽  
Duplex Dna ◽  
Dnaa Protein ◽  
Amino Terminal

The role of the C-terminal region of olive latent virus 1 coat protein in host systemic infection

2006 ◽  
Vol 151 (10) ◽  
pp. 1973-1983 ◽  
Author(s):  
V. Pantaleo ◽  
F. Grieco ◽  
A. Di Franco ◽  
G. P. Martelli
Keyword(s):  
Coat Protein ◽  
Systemic Infection ◽  
Terminal Region ◽  
Latent Virus

Role of vasostatin-1 C-terminal region in fibroblast cell adhesion

2010 ◽  
Vol 67 (12) ◽  
pp. 2107-2118 ◽  
Author(s):  
Eleonora Dondossola ◽  
Anna Gasparri ◽  
Angela Bachi ◽  
Renato Longhi ◽  
Marie-Hélène Metz-Boutigue ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Fibroblast Cell ◽  
Terminal Region

scholarly journals Role of the N-terminal region in covalent modification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: comparison of phosphorylation and ADP-ribosylation

1995 ◽  
Vol 309 (1) ◽  
pp. 119-125 ◽  
Author(s):  
J L Rosa ◽  
J X Pérez ◽  
F Ventura ◽  
A Tauler ◽  
J Gil ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Covalent Modification ◽  
Terminal Region ◽  
Bifunctional Enzyme ◽  
Dependent Protein Kinase ◽  
Adp Ribosylation ◽  
Camp Dependent Protein Kinase ◽  
Arginine Residues ◽  
Dependent Protein

The effect of cyclic AMP (cAMP)-dependent phosphorylation and ADP-ribosylation on the activities of the rat liver bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2), was investigated in order to determine the role of the N-terminus in covalent modification of the enzyme. The bifunctional enzyme was demonstrated to be a substrate in vitro for arginine-specific ADP-ribosyltransferase: 2 mol of ADP-ribose was incorporated per mol of subunit. The Km values for NAD+ and PFK-2/FBPase-2 were 14 microM and 0.4 microM respectively. A synthetic peptide (Val-Leu-Gln-Arg-Arg-Arg-Gly-Ser-Ser-Ile-Pro-Gln) corresponding to the site phosphorylated by cAMP-dependent protein kinase was ADP-ribosylated on all three arginine residues. Analysis of ADP-ribosylation of analogue peptides containing only two arginine residues, with the third replaced by alanine, revealed that ADP-ribosylation occurred predominantly on the two most C-terminal arginine residues. Sequencing of the ADP-ribosylated native enzyme also demonstrated that the preferred sites were at Arg-29 and Arg-30, which are just N-terminal to Ser-32, whose phosphorylation is catalysed by cAMP-dependent protein kinase (PKA). ADP-ribosylation was independent of the phosphorylation state of the enzyme. Furthermore, ADP-ribosylation of the enzyme decreased its recognition by liver-specific anti-bifunctional-enzyme antibodies directed to its unique N-terminal region. ADP-ribosylation of PFK-2/FBPase-2 blocked its phosphorylation by PKA, and decreased its PFK-2 activity, but did not alter FBPase-2 activity. In contrast, cAMP-dependent phosphorylation inhibited the kinase and activated the bisphosphatase. These results demonstrate that ADP-ribosylation of arginine residues just N-terminal to the site phosphorylated by PKA modulate PFK-2 activity by an electrostatic and/or steric mechanism which does not involved uncoupling of N- and C-terminal interactions as seen with cAMP-dependent phosphorylation.

Abstract 52: The Role of Kindlin-2 in Integrin Activation Depends on a Short C-Terminal Region

2012 ◽  
Vol 32 (suppl_1) ◽  
Author(s):  
Jamila Hirbawi ◽  
Kamila Bledzka ◽  
Yan Qing Ma ◽  
Jun Qin ◽  
Edward F Plow
Keyword(s):  
Amino Acids ◽  
Point Mutation ◽  
Single Point ◽  
Terminal Region ◽  
Membrane Receptors ◽  
Single Point Mutation ◽  
Loss Of Function ◽  
Integrin Activation ◽  
C Terminus

Integrins are heterodimeric cell membrane receptors that regulate cell adhesion, migration, and survival. The kindlins are known to be key regulators of integrin activation, the transition from a low affinity, default state to a high affinity state for ligand. This function depends on their binding, together with talin, to the cytoplasmic tails (CT) of the β subunit of integrins. Kindlins are FERM domain containing proteins, and it is its F3 (PTB) subdomain of the FERM that is the primary binding site for integrin β CT. At its very C-terminus, beyond the F3, is a short extension of 21 amino acids, K2 660-680, and we have focused on the role of this region in the co-activator function of kindlin-2 (K2). For this analysis, we performed PAC-1 (antibody to detect activated αIIbβ3 integrin) binding assays in CHO cells stably expressing integrin α IIb β 3 that were transiently transfected with talin head domain and K2 mutants. Expression levels of all proteins were verified to be similar by western blotting and FACS. Truncation of K2 at residue 660 essentially eliminated the co-activator function of K2. Deletion of smaller segments also reduced co-activator activity by 50% to 100%. Deletion of just the last two amino acids in the sequence, W 679 V 680 , resulted in a 50% reduction in co-activator activity and a single point mutation of Y 673 A also led to a 50% loss of function. A combination mutant consisting of the W 679 V 680 deletion and the Y 673 point mutation resulted in 100% loss of kindlin-2 co-activator activity. Pull-down experiments performed using GST tagged β 3 CT and CHO lysates transfected with GFP-kindlin-2 forms suggested that the C-terminal deletion did not disrupt binding to β 3 CT. This observation was corroborated by surface plasmon resonance studies in which the binding of full-length K2 and K2Δ666C (Δ666) was compared, and their K D values for immobilized β3 CT were found to be essentially the same. Overall, these data establish an important and unanticipated role of the carboxy-terminal region of kindlin-2 in its integrin co-activator function that is not dependent of its binding to integrin.

Tubulin folding is altered by mutations in a putative GTP binding motif

1996 ◽  
Vol 109 (6) ◽  
pp. 1471-1478 ◽  
Author(s):  
J.C. Zabala ◽  
A. Fontalba ◽  
J. Avila
Keyword(s):  
Intramolecular Interaction ◽  
Terminal Region ◽  
Binding Motif ◽  
Beta Tubulin ◽  
Alpha Tubulin ◽  
Proposed Model ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal ◽  
Hydrolysis Of

Tubulins contain a glycine-rich loop, that has been implicated in microtubule dynamics by means of an intramolecular interaction with the carboxy-terminal region. As a further extension of the analysis of the role of the carboxy-terminal region in tubulin folding we have mutated the glycine-rich loop of tubulin subunits. An alpha-tubulin point mutant with a T150-->G substitution (the corresponding residue present in beta-tubulin) was able to incorporate into dimers and microtubules. On the other hand, four beta-tubulin point mutants, including the G148-->T substitution, did not incorporate into dimers, did not release monomers, but were able to form C900 and C300 complexes (intermediates in the process of tubulin folding). Three other mutants within this region (which approximately encompasses residues 137–152) were incapable of forming dimers and C300 complexes but gave rise to the formation of C900 complexes. These results suggest that tubulin goes through two sequential folding states during the folding process, first in association with TCP1-complexes (C900) prior to the transfer to C300 complexes. It is this second step that implies binding/hydrolysis of GTP, reinforcing our previous proposed model for tubulin folding and assembly.

Structure, stability, and chaperone function of αA-crystallin: Role of N-terminal region

Biopolymers ◽  
2007 ◽  
Vol 86 (3) ◽  
pp. 177-192 ◽  
Author(s):  
Madhuchhanda Kundu ◽  
P. C. Sen ◽  
K. P. Das
Keyword(s):  
Terminal Region ◽  
Structure Stability ◽  
Chaperone Function
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