Protein NO52—a constitutive nucleolar component sharing high sequence homologies to protein NO66

2005 ◽  
Vol 84 (2-3) ◽  
pp. 279-294 ◽  
Author(s):  
Jens Eilbracht ◽  
Sandra Kneissel ◽  
Astrid Hofmann ◽  
Marion S. Schmidt-Zachmann
1977 ◽  
Vol 75 (4) ◽  
pp. 980-986 ◽  
Author(s):  
Andre Foriers ◽  
Christian Wuilmart ◽  
Nathan Sharon ◽  
A. Donny Strosberg

1984 ◽  
Vol 9 (6) ◽  
pp. 271-273 ◽  
Author(s):  
Jeremy N. Timmis ◽  
N. Steele Scott

1987 ◽  
Vol 15 (1) ◽  
pp. 67-85 ◽  
Author(s):  
Y.L. Yan ◽  
C.J. Kunert ◽  
J.H. Postlethwait
Keyword(s):  

1992 ◽  
Vol 6 (3) ◽  
pp. 235-252 ◽  
Author(s):  
David F. V. Lewis ◽  
Henri Moereels

1981 ◽  
Vol 195 (1) ◽  
pp. 31-40 ◽  
Author(s):  
F E Cohen ◽  
J Novotný ◽  
M J E Sternberg ◽  
D G Campbell ◽  
A F Williams

The Thy-1 membrane glycoprotein from rat brain is shown to have structural and sequence homologies with immunoglobulin (Ig) domains on the basis of the following evidence. 1. The two disulphide bonds of Thy-1 are both consistent with the Ig-fold. 2. The molecule contains extensive beta-structure as shown by the c.d. spectrum. 3. Secondary structure prediction locates beta-strands along the sequence in a manner consistent with the Ig-fold. 4. On the basis of rules derived from known beta-sheet structures, a three-dimensional structure with the Ig-fold is predicted as favourable for Thy-1. 5. Sequences in the proposed beta-strands of Thy-1 and known beta-strands of Ig domains show significant sequence homology. This homology is statistically more significant than for the comparison of proposed beta-strand sequences of beta 2-microglobulin with Ig domains. An hypothesis is presented for the possible functional significance of an evolutionary relationship between Thy-1 and Ig. It is suggested that both Thy-1 and Ig evolved from primitive molecules, with an Ig fold, which mediated cell--cell interactions. The present-day role of Thy-1 may be similar to that of the primitive domain.


1982 ◽  
Vol 10 (1) ◽  
pp. 365-374 ◽  
Author(s):  
Robert Harr ◽  
Per Hagblom ◽  
Petter Gustafsso

2005 ◽  
Vol 187 (4) ◽  
pp. 1293-1304 ◽  
Author(s):  
Mohamed Jebbar ◽  
Linda Sohn-Bösser ◽  
Erhard Bremer ◽  
Théophile Bernard ◽  
Carlos Blanco

ABSTRACT To understand the mechanisms of ectoine-induced osmoprotection in Sinorhizobium meliloti, a proteomic examination of S. meliloti cells grown in minimal medium supplemented with ectoine was undertaken. This revealed the induction of 10 proteins. The protein products of eight genes were identified by using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Five of these genes, with four other genes whose products were not detected on two-dimensional gels, belong to the same gene cluster, which is localized on the pSymB megaplasmid. Four of the nine genes encode the characteristic components of an ATP-binding cassette transporter that was named ehu, for ectoine/hydroxyectoine uptake. This transporter was encoded by four genes (ehuA, ehuB, ehuC, and ehuD) that formed an operon with another gene cluster that contains five genes, named eutABCDE for ectoine utilization. On the basis of sequence homologies, eutABCDE encode enzymes with putative and hypothetical functions in ectoine catabolism. Analysis of the properties of ehuA and eutA mutants suggests that S. meliloti possesses at least one additional ectoine catabolic pathway as well as a lower-affinity transport system for ectoine and hydroxyectoine. The expression of ehuB, as determined by measurements of UidA activity, was shown to be induced by ectoine and hydroxyectoine but not by glycine betaine or by high osmolality.


FEBS Letters ◽  
1985 ◽  
Vol 189 (1) ◽  
pp. 85-88 ◽  
Author(s):  
Reiko Kikuno ◽  
Takashi Miyata

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