A domain of the α-subunit of rabbit phosphorylase kinase shows homologies with regions of rabbit α-tropomyosin, human EGF receptor, and the α chain of bovine S-100 protein

1992 ◽  
Vol 12 (4) ◽  
pp. 313-317 ◽  
Author(s):  
Theodore G. Sotiroudis ◽  
Taxiarchis P. Geladopoulos
Keyword(s):  
Statistical Analysis ◽  
Amino Acid ◽  
Sequence Comparison ◽  
Egf Receptor ◽  
Phosphorylase Kinase ◽  
Α Subunit ◽  
Biological Implication ◽  
S 100 ◽  
Α Chain ◽  
Amino Acid Segment

Sequence comparison of the α-subunit of phosphorylase kinase with α-tropomyosin revealed 32% identity, and 49% similarity, between the region of α-tropomyosin coded by exon 5 and a 39 amino acid segment of the kinase subunit. A subsequence of the α-subunit segment and a sequence overlapping the same α-subunit region are homologous with: (a) a region of the cytoplasmic domain of EGF receptor (50% identity) and (b) a Ca2+-binding domain of the α chain of S-100 protei (50% identity) respectively. Statistical analysis shows that these homologies are significant. The biological implication of the above similarities is discussed.

scholarly journals The Amino Acid Sequence of the A Protein (α Subunit) of the Tryptophan Synthetase of Escherichia coli

1967 ◽  
Vol 242 (22) ◽  
pp. 5442-5446 ◽  
Author(s):  
John R. Guest ◽  
Gabriel R. Drapeau ◽  
Bruce C. Carlton ◽  
Charles Yanofsky
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Α Subunit ◽  
Tryptophan Synthetase

Streptokinase secretion by Serratia marcescens signaled by the C-terminal 41 amino acid segment of metalloprotease

IUBMB Life ◽  
1998 ◽  
Vol 45 (4) ◽  
pp. 725-733
Author(s):  
Ki Seok Kim ◽  
Kwang Hee Bae ◽  
Il Chul Kim ◽  
Si Myung Byun ◽  
Yong Chul Shin
Keyword(s):  
Amino Acid ◽  
Serratia Marcescens ◽  
Amino Acid Segment

scholarly journals Hsp90 Binds and Regulates the Ligand-Inducible α Subunit of Eukaryotic Translation Initiation Factor Kinase Gcn2

1999 ◽  
Vol 19 (12) ◽  
pp. 8422-8432 ◽  
Author(s):  
Olivier Donzé ◽  
Didier Picard
Keyword(s):  
Amino Acid ◽  
Constitutive Expression ◽  
Amino Acid Starvation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Restrictive Temperature ◽  
Α Subunit ◽  
Macbecin I

ABSTRACT The protein kinase Gcn2 stimulates translation of the yeast transcription factor Gcn4 upon amino acid starvation. Using genetic and biochemical approaches, we show that Gcn2 is regulated by the molecular chaperone Hsp90 in budding yeast Saccharomyces cerevisiae. Specifically, we found that (i) several Hsp90 mutant strains exhibit constitutive expression of a GCN4-lacZ reporter plasmid; (ii) Gcn2 and Hsp90 form a complex in vitro as well as in vivo; (iii) the specific inhibitors of Hsp90, geldanamycin and macbecin I, enhance the association of Gcn2 with Hsp90 and inhibit its kinase activity in vitro; (iv) in vivo, macbecin I strongly reduces the levels of Gcn2; (v) in a strain expressing the temperature-sensitive Hsp90 mutant G170D, both the accumulation and activity of Gcn2 are abolished at the restrictive temperature; and (vi) the Hsp90 cochaperones Cdc37, Sti1, and Sba1 are required for the response to amino acid starvation. Taken together, these data identify Gcn2 as a novel target for Hsp90, which plays a crucial role for the maturation and regulation of Gcn2.

Correction to the Amino Acid Sequence of the α Chain of Human Haptoglobin

1973 ◽  
Vol 51 (3) ◽  
pp. 321-322 ◽  
Author(s):  
B. Malchy ◽  
G. H. Dixon
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Α Chain

The previously published amino acid sequence of the α chain of human haptoglobin must be corrected to include a half-cystine residue at position 73.

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