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1  antibody, and tissue plasminogen activator (Activase).
2  activase but now fully activated by tobacco activase.
3 n state of Rubisco via inhibition of Rubisco activase.
4  dynein motor proteins, TorsinA, and Rubisco activase.
5 h activase but was well activated by tobacco activase.
6 acilitated activation by spinach and tobacco activase.
7 oenzyme that interacts directly with Rubisco activase.
8 ctivase was much more effective than tobacco activase.
9 be detached from the active sites by Rubisco activase.
10  of CbbX, the alpha-proteobacterial red-type activase.
11 l structure of the C-domain core of creosote activase.
12 e, the first structures of an AdoMet radical activase.
13 logous single and double mutations in cotton activase.
14 sco mutants, mimicking activation by spinach activase.
15 ter than tobacco Rubisco, similar to spinach activase.
16 her than for Antarctic hairgrass and spinach activase.
17 educing the activation of Rubisco by Rubisco activase.
18 imilar in function to pyruvate formate-lyase activase.
19 co) in vivo requires the presence of Rubisco activase, a nuclear-encoded chloroplast protein that con
20  the Sensor 2 domain of the tobacco chimeric activase abolished its ability to better activate spinac
21                In contrast, tobacco chimeric activase activated spinach Rubisco far better than tobac
22 pecificity from non-Solanaceae to Solanaceae activase activation.
23                                Thus, loss of activase activity during heat stress is caused by an exc
24  faster rate of deactivation, but by reduced activase activity possibly in response to unfavorable AT
25 etion of the first 50 amino acids of Rubisco activase almost completely eliminated the ability to act
26 ) complexes requires the activity of Rubisco activase, an AAA+ ATPase that utilizes chemo-mechanical
27 hat anaerobic ribonucleotide reductase (RNR) activase, an ancient enzyme that, it has been suggested,
28 n Arabidopsis clone (R100) with 30 to 40% Wt activase, an effect that was more pronounced in high lig
29      To examine interactions between Rubisco activase and ATP, site-directed mutations were made at t
30 res similar to those that denatured isolated activase and far below those required to denature Rubisc
31 egrees C, whereas the activities of isolated activase and Rubisco were highest at 42 degrees C and >5
32 l insights into the interactions between the activase and the G(734) loop of pyruvate formate-lyase a
33 roplastic (Rubisco small subunit and Rubisco activase) and peroxisomal (catalase) components of the p
34 ng complex binding proteins 1 and 3, Rubisco activase, and carbonic anhydrase.
35 nthetic enzymes, such as Rubisco and Rubisco activase, and enzymes of Suc biosynthesis such as Suc-ph
36 bisphosphate carboxylase/oxygenase (Rubisco) activase Arabidopsis thaliana with reduced concentration
37 nstrates for the first time that radical SAM activases are also capable of an alternative cleavage pa
38 d to date, there are two isoforms of Rubisco activase arising from alternative splicing that differ o
39 efine the size and function of this putative activase binding region, substitutions were created at p
40 isco was only partially activated by spinach activase but now fully activated by tobacco activase.
41 t, P89R Rubisco was not activated by spinach activase but was well activated by tobacco activase.
42  ability to regulate the activity of Rubisco activase by redox changes in the stroma.
43 ts into the mechanism of redox regulation of activase by the C-extension in the large isoform.
44                                              Activase content was 5% and 1.4% of total soluble protei
45                                      Tobacco activase does not markedly facilitate the activation of
46                                  The tobacco activase double mutant D311K/L314V activated wild type C
47 , K48- and K63-linked ubiquitination, and E1 activases, E2 conjugases, and E3 ligases involved in ubi
48 structural information for different Rubisco activase enzymes, the arrangement of these subunits in s
49                                     Isolated activase exhibited a temperature optimum for ATP hydroly
50                                      Rubisco activase facilitates this spontaneous carbamylation/meta
51 lamydomonas reinhardtii), and non-Solanaceae activase fails to activate Solanaceae Rubisco.
52 redoxin or ribulose-bisphosphate carboxylase activase for stromal targeting.
53 er Trial of EkoSonic Endovascular System and Activase for Treatment of Acute Pulmonary Embolism) to i
54 ive specificities of the spinach and tobacco activases for Chlamydomonas Rubisco were switched by cha
55 a variety of techniques to show that Rubisco activase forms a wide range of structures in solution, r
56    The data support a model in which Rubisco activase forms an open spiraling structure rather than a
57                                              Activase from Solanaceae plants (e.g. tobacco) fails to
58 hanging a Sensor 2-containing region between activases from spinach and tobacco.
59                      To determine if loss of activase function is caused by protein denaturation, the
60  the maximal activity of the enzyme, Rubisco activase has an oligomeric state of 2-4 subunits.
61 at-treated activase trapped partially folded activase in an insoluble complex at treatment temperatur
62  of the N-terminal region of tobacco Rubisco activase in ATP hydrolysis and ribulose-1,5-bisphosphate
63 that Wt Arabidopsis does not contain Rubisco activase in great excess of the amount required for opti
64                              Role of Rubisco Activase in imparting thermotolerance to the photosynthe
65             These results support a role for activase in limiting photosynthesis at high temperature.
66 ccurred at 45 degrees C and 37 degrees C for activase in the presence and absence of ATPgammaS, respe
67 eriments showed that thermal denaturation of activase in vivo occurred at temperatures similar to tho
68 identified a substrate recognition region in activase in which two residues may directly interact wit
69                                      Rubisco activase is a nuclear-encoded chloroplast protein that i
70                                      Rubisco activase is an AAA(+) protein, a superfamily with member
71                                      Rubisco activase is an essential enzyme for photosynthesis, whic
72              Thus, the N-terminus of Rubisco activase is distinct from the ATP-hydrolyzing domain and
73 To determine whether the analogous domain of activase is involved in recognition of ribulose-1,5-bisp
74                                              Activase is thought to play a central role in coordinati
75 d by a radical S-adenosyl-L-methionine (SAM) activase, is a simple and effective catalyst, but is als
76 e that the C-extension of the oxidized large activase isoform can be cross-linked with regions contai
77 to redox regulate the activity of the larger activase isoform was eliminated by replacement of the cr
78                            In the absence of activase, isolated Rubisco deactivated under catalytic c
79 uces oligomeric transitions to the bacterial activase, it merely enhances the kinetics of ATP hydroly
80 ohydrate distribution and influences Rubisco activase levels.
81      In cyanobacteria, a homologous protein (activase-like cyanobacterial protein, ALC), contains a d
82 enetic basis for the function of the Rubisco activase-like gene (rca) was sought.
83 r, are not prone to inhibition, and often no activase machinery is associated with these enzymes.
84 lomerata express Dgrca (D. glomerata Rubisco activase) mRNA, a transcript usually associated with pho
85               The ability of the two tobacco activase mutants to activate wild type and mutant Chlamy
86                         KEY MESSAGE: Rubisco activase of plants evolved in a stepwise manner without
87  not D94K Rubisco, whereas the tobacco L314V activase only activated D94K Rubisco.
88 erefore, we speculate that upon binding, the activase paddles embrace the Rubisco cylinder by placing
89                                          The activase performs this remarkable feat by using an iron-
90  was associated with the expression of a new activase polypeptide.
91 posite mutation, D311K, in wild type tobacco activase produced an enzyme that activated both spinach
92 dation also modulated the activity of native activase proteins isolated from either Arabidopsis or sp
93 tivity is regulated by its chaperone Rubisco activase (Rca) and by adjustments in the chloroplast str
94 in and essential molecular chaperone Rubisco activase (Rca) constantly remodels inhibited active site
95 at) genome encodes three isoforms of Rubisco activase (Rca) differing in thermostability, which could
96                                      Rubisco activase (Rca) facilitates the release of sugar-phosphat
97                                  The Rubisco activase (RCA) gene from each species was sequenced.
98 ance of the heat-sensitive chaperone Rubisco activase (Rca) in each species.
99 ed the mechanism of the AAA+ protein Rubisco activase (Rca) in metabolic repair of the photosynthetic
100 bisphosphate carboxylase/oxygenase (Rubisco) activase (Rca) is a AAA(+) enzyme that uses ATP to remov
101                                      Rubisco activase (Rca) is a key molecular chaperone that maintai
102 iosphere, by its molecular chaperone Rubisco activase (Rca) is essential for photosynthesis and plant
103 bisphosphate carboxylase/oxygenase (Rubisco) activase (RCA) is organ-specific, light-responsive, and
104                          Arabidopsis Rubisco activase (Rca) is phosphorylated at threonine-78 (Thr78)
105 ion inhibition due to heat sensitive Rubisco activase (RCA) is the most prominent.
106     This process frequently requires rubisco activase (Rca) machinery, which couples ATP hydrolysis t
107 ulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) promotes the onset of basal dark-induced
108                           In plants, rubisco activase (Rca) regulates rubisco by removing inhibitory
109 eactivation due to the inhibition of Rubisco activase (RCA) under moderately elevated temperatures.
110 TP-synthase gamma-subunit (AtpC) and Rubisco activase (RCA) were identified by matrix-assisted laser-
111       Rubisco's catalytic chaperone, Rubisco activase (Rca), uses the energy from ATP hydrolysis to r
112 osynthesis, Rubisco, is regulated by Rubisco activase (Rca).
113 remodeled by the molecular chaperone Rubisco activase (Rca).
114 rs are released by the motor protein Rubisco activase (Rca).
115 ested this method on the AAA+ ATPase Rubisco activase (Rca).
116 omonas reinhardtii mutant that lacks Rubisco activase (Rca).
117 ar activities (AAA+ proteins) termed Rubisco activases (Rcas).
118 iverse molecular chaperones known as rubisco activases (Rcas).
119 iverse molecular chaperones known as Rubisco activases (Rcas).
120                                Tobacco D311K activase readily activated wild type and P89R but not D9
121  in plants containing both isoforms, Rubisco activase regulates the activity of Rubisco in response t
122 psis thaliana with reduced concentrations of activase relative to wild-type (Wt) plants were measured
123          We propose a model in which Rubisco activase requires at least 1 neighboring subunit for hyd
124                         The proteins Rubisco activase, Rubisco, and the 33-kD O2-evolving complex sub
125               In an attempt to eliminate the activase/Rubisco interaction, proline 89 was changed to
126                               Increasing the activase/Rubisco ratio reduced Rubisco deactivation at h
127    This substitution also caused reversal of activase specificity, indicating that amino acid identit
128  for the pronounced cooperativity of Rubisco activase subunits, we suggest that coordination of the A
129                   We show that the two CbbQO activase systems display specificity for the rubisco enz
130 was estimated at 20 Rubisco active sites per activase tetramer in Wt Arabidopsis and 60 to 80 in the
131  results are consistent with a mechanism for activase that involves ATP-binding, subunit aggregation
132 in the three C4 crops indicated that Rubisco activase, the pyruvate phosphate dikinase regulatory pro
133 sis, oxidation of the large (46-kDa) isoform activase to form a disulfide bond in the C-terminal exte
134                               The ability of activase to maintain or promote Rubisco activation in vi
135 s been attributed to an inability of Rubisco activase to maintain Rubisco in an active form.
136 Rubisco deactivation exceeds the capacity of activase to promote activation.
137 nt tissue-type plasminogen activator (rt-PA, Activase) to methionine oxidation when treated with the
138                            In Salix, Rubisco activase transcripts were down-regulated in contaminated
139 emically denatured rhodanese to heat-treated activase trapped partially folded activase in an insolub
140                                 Ubiquitin E1 activase UBA (ubiquitin activating enzyme)-6 and E3 liga
141 hizophrenia, with decreased levels of the E1 activase UBA3 and the E3 ligase Rnf7.
142 bisphosphate carboxylase/oxygenase (Rubisco) activase uses the energy from ATP hydrolysis to remove t
143 combinant creosote bush, cotton, and tobacco activase was 8 degrees C to 10 degrees C higher than for
144                             Spinach chimeric activase was a poor activator of both spinach and tobacc
145              The stoichiometry of Rubisco to activase was estimated at 20 Rubisco active sites per ac
146 otein denaturation, the thermal stability of activase was examined in vitro and in vivo and compared
147 d K356Q Rubisco were similar in that spinach activase was much more effective than tobacco activase.
148 cv "Little Marvel") chloroplasts showed that activase was the major protein that denatured in respons
149 (2)), the metabolic repair protein RsRca (Rs-activase) was introduced via nuclear transformation.
150 ase (Rubisco), which is regulated by Rubisco activase, was closely correlated with temperature-induce
151 e, and the activities of Rubisco and Rubisco activase were examined in species from contrasting envir
152 ygenase (Rubisco, EC 4.1.1.39), two chimeric activases were constructed, interchanging a Sensor 2-con
153 ested that there are two isoforms of Rubisco activase which may provide an explanation for the abilit
154 ter by recombinant Arabidopsis 43-kD Rubisco activase with the amino acid replacements Q111E and Q111

 
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