scholarly journals Crystal structure of the PH1932 protein, a unique archaeal ArsR type winged-HTH transcription factor from Pyrococcus horikoshii OT3

2007 ◽  
Vol 70 (4) ◽  
pp. 1631-1634 ◽  
Author(s):  
Hiroshi Itou ◽  
Min Yao ◽  
Nobuhisa Watanabe ◽  
Isao Tanaka
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Protein A ◽  
Pyrococcus Horikoshii

scholarly journals Compromised Function of the Pancreatic Transcription Factor PDX1 in a Lineage of Desert Rodents

2021 ◽  
Author(s):  
Yichen Dai ◽  
Sonia Trigueros ◽  
Peter W. H. Holland
Keyword(s):  
Transcription Factor ◽  
Gene Conversion ◽  
Cell Function ◽  
Protein A ◽  
Gene Promoter ◽  
Homeodomain Protein ◽  
Β Cell ◽  
Desert Rodents ◽  
Biased Gene Conversion ◽  
Β Cell Function

AbstractGerbils are a subfamily of rodents living in arid regions of Asia and Africa. Recent studies have shown that several gerbil species have unusual amino acid changes in the PDX1 protein, a homeodomain transcription factor essential for pancreatic development and β-cell function. These changes were linked to strong GC-bias in the genome that may be caused by GC-biased gene conversion, and it has been hypothesized that this caused accumulation of deleterious changes. Here we use two approaches to examine if the unusual changes are adaptive or deleterious. First, we compare PDX1 protein sequences between 38 rodents to test for association with habitat. We show the PDX1 homeodomain is almost totally conserved in rodents, apart from gerbils, regardless of habitat. Second, we use ectopic gene overexpression and gene editing in cell culture to compare functional properties of PDX1 proteins. We show that the divergent gerbil PDX1 protein inefficiently binds an insulin gene promoter and ineffectively regulates insulin expression in response to high glucose in rat cells. The protein has, however, retained the ability to regulate some other β-cell genes. We suggest that during the evolution of gerbils, the selection-blind process of biased gene conversion pushed fixation of mutations adversely affecting function of a normally conserved homeodomain protein. We argue these changes were not entirely adaptive and may be associated with metabolic disorders in gerbil species on high carbohydrate diets. This unusual pattern of molecular evolution could have had a constraining effect on habitat and diet choice in the gerbil lineage.

scholarly journals Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.

1990 ◽  
Vol 87 (12) ◽  
pp. 4849-4853 ◽  
Author(s):  
A. T. Brunger ◽  
M. V. Milburn ◽  
L. Tong ◽  
A. M. deVos ◽  
J. Jancarik ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Active Form ◽  
Protein A ◽  
Ras Protein

scholarly journals Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 Å resolution

2004 ◽  
Vol 58 (3) ◽  
pp. 769-773 ◽  
Author(s):  
Neratur K. Lokanath ◽  
Chizu Kuroishi ◽  
Nobuo Okazaki ◽  
Naoki Kunishima
Keyword(s):  
Crystal Structure ◽  
Glycine Cleavage System ◽  
Pyrococcus Horikoshii ◽  
Glycine Cleavage

scholarly journals The X-ray crystal structure of PA1607 from Pseudomonas aureginosa at 1.9 A resolution--a putative transcription factor

2007 ◽  
Vol 16 (3) ◽  
pp. 543-549 ◽  
Author(s):  
E. A.L. Sieminska ◽  
X. Xu ◽  
A. Savchenko ◽  
D. A.R. Sanders
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
X Ray ◽  
Putative Transcription Factor

scholarly journals Erratum: The crystal structure of d(GGATGGGAG): an essential part of the binding site for transcription factor IIIA

Nature ◽  
1986 ◽  
Vol 323 (6084) ◽  
pp. 184-184
Author(s):  
M. McCall ◽  
T. Brown ◽  
W. N. Hunter ◽  
O. Kennard
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Binding Site ◽  
Transcription Factor Iiia

scholarly journals A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts

2020 ◽  
Author(s):  
Charles R Midgett ◽  
Rachel A Swindell ◽  
Maria Pellegrini ◽  
F Jon Kull
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Disulfide Bond ◽  
Bile Salts ◽  
Biochemical Analysis ◽  
Conformation Analysis ◽  
Binding Partner ◽  
Bile Resistance ◽  
Periplasmic Domain

AbstractToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrio family. In some pathogenic Vibrios, including V. parahaemolyticus and V. cholerae, ToxR is required for bile resistance and virulence, and ToxR is fully activated and protected from degradation by ToxS. ToxS achieves this in part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of ToxR (dbToxRp). In this study, biochemical analysis showed dbToxRp to have a higher affinity for the ToxS periplasmic domain than the non-disulfide bonded conformation. Analysis of our dbToxRp crystal structure showed this is due to disulfide bond stabilization. Furthermore, dbToxRp is structurally homologous to the V. parahaemolyticus VtrA periplasmic domain. These results highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a domain fold involved in environmental sensing conserved across the Vibrio family.

scholarly journals Crystal Structure of FolD Bifunctional Protein, a Methylenetetrahydrofolate Dehydrogenase/Cyclohydrolase from Campylobacter jejuni

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Magdalena Maria Makowska‐Grzyska ◽  
Rongguang Zhang ◽  
Scott N Peterson ◽  
Andrzej Joachimiak
Keyword(s):  
Crystal Structure ◽  
Campylobacter Jejuni ◽  
Protein A ◽  
Bifunctional Protein ◽  
Methylenetetrahydrofolate Dehydrogenase

scholarly journals Non-p53 p53RE binding protein, a human transcription factor functionally analogous to P53

1998 ◽  
Vol 95 (12) ◽  
pp. 6681-6686 ◽  
Author(s):  
X. Zeng ◽  
A. J. Levine ◽  
H. Lu
Keyword(s):  
Transcription Factor ◽  
Binding Protein ◽  
Protein A ◽  
Human Transcription Factor
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