Erratum to “Ni(II) and Cu(II) Binding with a 14-aminoacid Sequence of Cap43 protein, TRSRSHTSEGTRSR”

2002 ◽  
Vol 91 (2) ◽  
pp. 421
Author(s):  
Maria Antonietta Zoroddu ◽  
Teresa Kowalik-Jankowska ◽  
Henryk Kozlowski ◽  
Konstantin Salnikow ◽  
Max Costa
Keyword(s):  
Aminoacid Sequence

scholarly journals Aminoacid Sequence of Dogfish M4 Lactate Dehydrogenase

1973 ◽  
Vol 70 (6) ◽  
pp. 1790-1793 ◽  
Author(s):  
S. S. Taylor ◽  
S. S. Oxley ◽  
W. S. Allison ◽  
N. O. Kaplan
Keyword(s):  
Lactate Dehydrogenase ◽  
Aminoacid Sequence

scholarly journals The nucleoid as a scaffold for the assembly of bacterial signaling complexes

2017 ◽  
Author(s):  
Audrey Moine ◽  
Leon Espinosa ◽  
Eugenie Martineau ◽  
Mutum Yaikhomba ◽  
P J Jazleena ◽  
...  
Keyword(s):  
Dna Binding ◽  
Independent Manner ◽  
Signaling Systems ◽  
Bacterial Signaling ◽  
Aminoacid Sequence ◽  
Membrane Bound ◽  
Gliding Bacterium ◽  
Positively Charged

ABSTRACTThe FrzCD chemoreceptor from the gliding bacterium Myxococcus xanthus forms cytoplasmic clusters that occupy a large central region of the cell body also occupied by the nucleoid. In this work, we show that FrzCD directly binds to the nucleoid with its N-terminal positively charged tail and recruits active signaling complexes at this location. The FrzCD binding to the nucleoid occur in a DNA-sequence independent manner and leads to the formation of multiple distributed clusters that explore constrained areas. This organization might be required for cooperative interactions between clustered receptors as observed in membrane-bound chemosensory arrays.AUTHOR SUMMARYIn this work, we show that the cytoplasmic chemoreceptor of the Frz chemosensory system, FrzCD, does not bind the cytoplasmic membrane like most MCPs but bind the bacterial nucleoid directly, thus forming distributed protein clusters also containing the Frz kinase. In vitro and in vivo experiments show that DNA-binding is not sequence-specific and is mediated by a basic aminoacid sequence of the FrzCD N-terminal domain. The deletion of this motif abolishes FrzCD DNA-binding and cooperativity in the response to signals. This work shows the importance of the nucleoid in the organization and functioning of cytoplasmic signaling systems in bacteria.

scholarly journals Piezo1 forms a slowly-inactivating mechanosensory channel in mouse embryonic stem cells

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Josefina Inés del Mármol ◽  
Kouki K Touhara ◽  
Gist Croft ◽  
Roderick MacKinnon
Keyword(s):  
Motor Neurons ◽  
Es Cells ◽  
Embryonic Stem ◽  
Inactivation Kinetics ◽  
Fast Inactivation ◽  
Cell Stage ◽  
Slow Kinetics ◽  
Aminoacid Sequence ◽  
Reduced Rate ◽  
Mes Cells

Piezo1 is a mechanosensitive (MS) ion channel with characteristic fast-inactivation kinetics. We found a slowly-inactivating MS current in mouse embryonic stem (mES) cells and characterized it throughout their differentiation into motor-neurons to investigate its components. MS currents were large and slowly-inactivating in the stem-cell stage, and became smaller and faster-inactivating throughout the differentiation. We found that Piezo1 is expressed in mES cells, and its knockout abolishes MS currents, indicating that the slowly-inactivating current in mES cells is carried by Piezo1. To further investigate its slow inactivation in these cells, we cloned Piezo1 cDNA from mES cells and found that it displays fast-inactivation kinetics in heterologous expression, indicating that sources of modulation other than the aminoacid sequence determine its slow kinetics in mES cells. Finally, we report that Piezo1 knockout ES cells showed a reduced rate of proliferation but no significant differences in other markers of pluripotency and differentiation.

Ultrastructure of Two Mutants in the H-Subunit of Recombinant Human Ferritin: Ordered Arrays Indicate Altered Surface Properties

1990 ◽  
Vol 48 (1) ◽  
pp. 288-289
Author(s):  
William H. Massover ◽  
Sonia Levi ◽  
Alessandra Luzzago ◽  
Paola Tateo ◽  
Paolo Arosio
Keyword(s):  
Carbon Film ◽  
Iron Storage ◽  
E Coli ◽  
Thin Carbon ◽  
Aminoacid Sequence ◽  
Thin Carbon Film ◽  
Human Ferritin ◽  
Altered Surface ◽  
And Function ◽  
Molecular Structure And Function

Two major types of polypeptide subunits, H and L, coassemble (n = 24) as heteropolymers to form molecules of the iron-storage protein, ferritin [1]. The significance of the H-type subunits for molecular structure and function remains unclear. The present study has examined the ultrastructure of recombinant human ferritins which are homopolymers of wild-type or mutant H-subunits [2]. Both mutations change the aminoacid sequence along the outer surface of the molecule; 9Cd has a single substitution of glycine for the lysine at position 86, and Ml has a duplication of 18 aminoacids [2].Recombinant ferritins were overexpressed in E. coli. and purified as described by Levi et al [2]. Samples (0.1-0.5 mg/ml) were deposited onto a thin carbon film stripped from freshly cleaved mica and carried on 400 mesh grids; these specimen carriers had been made hydrophilic by glow discharge treatment. After negative staining with 2% sodium silicotungstate (pH 7.0), the specimens were dried and examined at lOOkV with a JEOL 100CX electron microscope.

Dominique Lambert, René Resöhazy. Comment les pattes viennent au serpent. Essai sur l'etonnante plasticite du vivant

1970 ◽  
Vol 10 (1) ◽  
pp. 278-280
Author(s):  
Piotr Lenartowicz
Keyword(s):  
Research Program ◽  
Base Pair ◽  
Philosophical Tradition ◽  
Embryological Development ◽  
Developmental Processes ◽  
Structural Identity ◽  
Aminoacid Sequence ◽  
Pierre Teilhard De Chardin ◽  
Evo Devo ◽  
Double Origin

The general ideas of this book are of double origin. One source is akin to the relatively recent current of biological thought named Evo-Devo. Second source belongs to a more ancient French philosophical tradition represented, among others, by Bergson and Pierre Teilhard de Chardin. Few words about the Evo-Devo research program. Its creation was prompted by the analysis of the developmental processes in the embryos of different species. About fifteen years ago some discoveries related to the dynamics of the embryological development demonstrated a striking structural identity/stability of homeoboxes in different living forms. Homeoboxes are just small genes (only 180 base pair long) determining a strictly specific aminoacid sequence of short polypeptides (only about 60 aminoacids long) which „act" like hormones, „regulating" the dynamism of the gradually developing body. The parentheses were used deliberately, to stress the arbitrary character of the „signalling".

Identification of neurophysins: Complete aminoacid sequence of horse VLDV-neurophysin

1981 ◽  
Vol 100 (2) ◽  
pp. 600-605 ◽  
Author(s):  
Marie-Thérèse Chauvet ◽  
Jacqueline Chauvet ◽  
Roger Acher
Keyword(s):  
Aminoacid Sequence

Purification and Characterization of Hepatic P-450Iie1 from Acetone-Treated Mice

1993 ◽  
Vol 9 (3) ◽  
pp. 539-546 ◽  
Author(s):  
Vincenzo Longo ◽  
Silvia Menicagli ◽  
Michael Minks ◽  
Annalisa Santucci ◽  
Pier Giovanni Gervasi
Keyword(s):  
Polyclonal Antibodies ◽  
High Spin State ◽  
Purification And Characterization ◽  
Turnover Number ◽  
High Turnover ◽  
Hepatic Microsomes ◽  
Aminoacid Sequence ◽  
Reconstituted System ◽  
Cytochrome P 450

A new cytochrome P-450 isozyme (Mr = 52,000) was purified to apparent electrophoretic homogeneity from hepatic microsomes of mice treated with acetone and its biochemical, spectral, and immunological properties characterized. Several criteria indicated that the purified cytochrome was distinct from the known mouse P-450 isozymes. The absolute spectrum of its oxidized form indicated that it was in the high spin state. In a reconstituted system, it showed low catalytic activities towards 7-ethoxycoumarin, aminopyrine, and coumarin, whereas it catalyzed the oxidation of aniline, acetone, dimelhylnitrosoamine with high turnover number. The mouse enzyme was immunoreactive with polyclonal antibodies against rat P-45011E1 and exhibited an NH2-terminal aminoacid sequence with a high homology to that of rat-P-450IIEI. Based upon the above catalytic, spectral, immunological and structural properties, the purified mouse P-450 appears to be the ortholog of previously described P-450IIE1 (s) of other species.

ChemInform Abstract: AMINOACID SEQUENCE OF VIOMYCIN

1973 ◽  
Vol 4 (33) ◽  
pp. no-no
Author(s):  
LESZEK LECHOWSKI
Keyword(s):  
Aminoacid Sequence
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