Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence

Biochemistry ◽  
1986 ◽  
Vol 25 (20) ◽  
pp. 6244-6251 ◽  
Author(s):  
Markku S. Kulomaa ◽  
Nancy L. Weigel ◽  
Don A. Kleinsek ◽  
Wanda G. Beattie ◽  
Orla M. Conneely ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Complementary Dna ◽  
Dna Nucleotide Sequence

scholarly journals Terminal deoxynucleotidyltransferase. Alignment of α- and β-subunits of the core enzyme along the primary translation product

1985 ◽  
Vol 227 (3) ◽  
pp. 1003-1007 ◽  
Author(s):  
C M Beach ◽  
S K Chan ◽  
T C Vanaman ◽  
M S Coleman
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Beta Subunits ◽  
Isolation And Purification ◽  
C Terminus ◽  
Human Lymphoblast ◽  
Catalytically Active ◽  
Single Polypeptide ◽  
Dna Nucleotide Sequence

Terminal deoxynucleotidyltransferase exists in multiple Mr forms, all apparently generated from a single polypeptide of 62kDa. On isolation and purification, the smallest catalytically active protein of this enzyme consists of two subunits, alpha (12kDa) and beta (30kDa). Recently a complementary-DNA nucleotide sequence has been reported for a portion of the enzyme from human lymphoblast. We have pinpointed the locations of the alpha- and beta-subunits within the elucidated nucleotide sequence. From these data, the portions of the nucleotide sequence coding for the catalytically important area of the transferase can be estimated. Here the amino acid sequence of a number of tryptic peptides from calf alpha- and beta-subunits is presented. Because of the striking homology between the amino acid sequence of the calf enzyme and that predicted for human lymphoblast enzyme, it is possible for us to conclude that the alpha-subunit was generated from the C-terminus of the precursor protein and the beta-subunit was non-overlapping and proximal.

Purification of a mature form of 60kDa heat-shock protein (chaperonin homolog) from porcine kidney and its partial amino acid sequence

1992 ◽  
Vol 24 (9) ◽  
pp. 1507-1510 ◽  
Author(s):  
Wakui Hideki ◽  
Itoh Hideaki ◽  
Tashima Yohtalou ◽  
Kobayashi Ryoji ◽  
Nakamoto Yasushi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Porcine Kidney ◽  
Partial Amino Acid Sequence ◽  
Mature Form

Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylase

Biochemistry ◽  
1985 ◽  
Vol 24 (3) ◽  
pp. 556-561 ◽  
Author(s):  
Simon C. M. Kwok ◽  
Fred D. Ledley ◽  
Anthony G. DiLella ◽  
Kathryn J. H. Robson ◽  
Savio L. C. Woo
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Phenylalanine Hydroxylase ◽  
Full Length ◽  
Complementary Dna ◽  
Human Phenylalanine Hydroxylase

scholarly journals HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts.

1991 ◽  
Vol 11 (8) ◽  
pp. 4036-4044 ◽  
Author(s):  
K Hirayoshi ◽  
H Kudo ◽  
H Takechi ◽  
A Nakai ◽  
A Iwamatsu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Heat Shock Protein ◽  
Chicken Embryo ◽  
Noncoding Region ◽  
Isolation And Characterization ◽  
Embryo Fibroblasts ◽  
Retention Signal ◽  
Chicken Embryo Fibroblasts

We report the isolation and characterization of a cDNA clone encoding HSP47, a transformation-sensitive heat shock protein that binds to collagen. A cDNA library was prepared from total RNA isolated from heat-shocked chicken embryo fibroblasts and screened by using oligonucleotide mixtures prepared on the basis of the N-terminal amino acid sequence of biochemically purified HSP47. The cDNA insert contained 3,278 bp, which encoded a 15-amino-acid signal peptide and a mature protein coding region consisting of 390 amino acid residues; it also included part of the 5' noncoding region and a long 3' noncoding region. The deduced amino acid sequence revealed an RDEL sequence at the C terminus, which is a variant of the KDEL retention signal for retention of proteins in the endoplasmic reticulum. Northern (RNA) blot analyses and nuclear run-on assays established that the induction of HSP47 by heat shock and its suppression after transformation of chicken embryo fibroblasts by Rous sarcoma virus are regulated at the transcriptional level. A homology search revealed that this protein belongs to the serpin family, the superfamily of plasma serine protease inhibitors. Although structurally homologous to the serpins, HSP47 lacks the active site thought to be essential for the inhibition of proteases and does not appear to bind to intracellular proteases. HSP47 is the first heat shock protein found to be a member of the serpin superfamily. Conversely, it is the first serpin family member that is not secreted from cells, which could be explained by acquisition of the RDEL retention signal during evolution.

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