scholarly journals Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the essential light chain.

1988 ◽  
Vol 8 (2) ◽  
pp. 794-801 ◽  
Author(s):  
R L Chisholm ◽  
A M Rushforth ◽  
R S Pollenz ◽  
E R Kuczmarski ◽  
S R Tafuri
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dictyostelium Discoideum ◽  
Light Chain ◽  
Single Gene ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Essential Light Chain ◽  
Isolation And Characterization

We used an antibody specific for Dictyostelium discoideum myosin to screen a lambda gt11 cDNA expression library to obtain cDNA clones which encode the Dictyostelium essential myosin light chain (EMLC). The amino acid sequence predicted from the sequence of the cDNA clone showed 31.5% identity with the amino acid sequence of the chicken EMLC. Comparisons of the Dictyostelium EMLC, a nonmuscle cell type, with EMLC sequences from similar MLCs of skeletal- and smooth-muscle origin, showed distinct regions of homology. Much of the observed homology was localized to regions corresponding to consensus Ca2+-binding of E-F hand domains. Southern blot analysis suggested that the Dictyostelium genome contains a single gene encoding the EMLC. Examination of the pattern of EMLC mRNA expression showed that a significant increase in EMLC message levels occurred during the first few hours of development, coinciding with increased actin expression and immediately preceding the period of maximal chemotactic activity.

Dictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the essential light chain

1988 ◽  
Vol 8 (2) ◽  
pp. 794-801
Author(s):  
R L Chisholm ◽  
A M Rushforth ◽  
R S Pollenz ◽  
E R Kuczmarski ◽  
S R Tafuri
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dictyostelium Discoideum ◽  
Light Chain ◽  
Single Gene ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Essential Light Chain ◽  
Isolation And Characterization

We used an antibody specific for Dictyostelium discoideum myosin to screen a lambda gt11 cDNA expression library to obtain cDNA clones which encode the Dictyostelium essential myosin light chain (EMLC). The amino acid sequence predicted from the sequence of the cDNA clone showed 31.5% identity with the amino acid sequence of the chicken EMLC. Comparisons of the Dictyostelium EMLC, a nonmuscle cell type, with EMLC sequences from similar MLCs of skeletal- and smooth-muscle origin, showed distinct regions of homology. Much of the observed homology was localized to regions corresponding to consensus Ca2+-binding of E-F hand domains. Southern blot analysis suggested that the Dictyostelium genome contains a single gene encoding the EMLC. Examination of the pattern of EMLC mRNA expression showed that a significant increase in EMLC message levels occurred during the first few hours of development, coinciding with increased actin expression and immediately preceding the period of maximal chemotactic activity.

scholarly journals Structural features of the low-molecular-mass human salivary mucin

1992 ◽  
Vol 287 (2) ◽  
pp. 639-643 ◽  
Author(s):  
M S Reddy ◽  
L A Bobek ◽  
G G Haraszthy ◽  
A R Biesbrock ◽  
M J Levine
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Structural Features ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Expression Library ◽  
Mrna Species ◽  
Salivary Mucin

The low-molecular-mass human salivary mucin has at least two isoforms, MG2a and MG2b, that differ primarily in their sialic acid and fucose content. In this study, we characterize further these isoforms, particularly their peptide moieties. Trypsin digests of MG2a and MG2b yielded high- and low-molecular-mass glycopeptides following gel filtration on Sephacryl S-300. The larger glycopeptides from MG2a and MG2b had similar amino acid compositions and identical N-terminal sequences, suggesting common structural features between their peptides. An oligonucleotide probe generated from the amino acid sequence of the smaller glycopeptide from MG2a was employed in Northern-blot analysis. This probe specifically hybridized to two mRNA species from human submandibular and sublingual glands. A cDNA clone selected from a human submandibular gland cDNA expression library with antibody generated against deglycosylated MG2a also hybridized to these two mRNA species. In both cases, the larger mRNA was polydisperse, and the hybridization signal was more intense in the sublingual gland. In addition, the N-terminal amino acid sequence of the larger glycopeptide was found to be part of one of the selected MG2 cDNA clones.

Amino Acid Sequence of the Essential Light Chain of Adductor Muscle Myosin from Ezo Giant Scallop, Patinopecten yessoensis1

1987 ◽  
Vol 102 (5) ◽  
pp. 1141-1149 ◽  
Author(s):  
Tetsuo MAITA ◽  
Kunihiko KONNO ◽  
Shinsaku MARUTA ◽  
Hajime NORISUE ◽  
Genji MATSUDA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Adductor Muscle ◽  
Essential Light Chain ◽  
Muscle Myosin

scholarly journals Human myeloperoxidase gene: molecular cloning and expression in leukemic cells

Blood ◽  
1986 ◽  
Vol 68 (6) ◽  
pp. 1411-1414
Author(s):  
KS Chang ◽  
JM Trujillo ◽  
RG Cook ◽  
SA Stass
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Clone ◽  
Northern Blot ◽  
Single Gene ◽  
Myelogenous Leukemia ◽  
Cloning And Expression ◽  
Leukemic Cells ◽  
Expression Library

We have molecularly cloned the human myeloperoxidase (MPO) gene from the lambda gt11 expression library by screening with an affinity- purified MPO antibody. The cDNA clone of the MPO gene was used to study MPO gene expression in leukemic cells. The amino acid sequence predicted from the nucleotide sequence of the cDNA clone pMP401 matched exactly the 23 amino acid sequence of the NH2-terminal of the 60,000 MPO subunit. We found that MPO cDNA hybridized to a single EcoRI genomic band of 19 kb, indicating that the MPO gene represents a single gene in the human genome. Northern blot analysis of RNA isolated from leukemic cell lines and acute myelogenous leukemia (AML) patients' samples shows that MPO gene expression correlated with myeloid lineage. The intensity of MPO mRNA expression on Northern blot correlated with the level of MPO expression by cytochemical staining. Multiple species of MPO mRNA were found. This indicates that a single MPO gene may encode different RNA species through a mechanism of posttranscriptional processing or that multiple transcriptional start/termination sites exist in the MPO gene.

Amino acid sequence of myosin essential light chain from the scallop Aquipecten irradians

Biochemistry ◽  
1986 ◽  
Vol 25 (23) ◽  
pp. 7651-7656 ◽  
Author(s):  
John H. Collins ◽  
John Kendrick-Jones ◽  
Ross Jakes ◽  
John Leszyk ◽  
Winifred Barouch ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Essential Light Chain

scholarly journals Characterization of primary amino acid sequence of human complement control protein factor I from an analysis of cDNA clones

1987 ◽  
Vol 242 (3) ◽  
pp. 849-856 ◽  
Author(s):  
C F Catterall ◽  
A Lyons ◽  
R B Sim ◽  
A J Day ◽  
T J R Harris
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Light Chain ◽  
Cdna Clones ◽  
Serine Proteinases ◽  
Human Complement ◽  
Factor I ◽  
Protein Factor ◽  
Control Protein

A cDNA clone of the mRNA coding for the human complement system control protein Factor I has been isolated. The predicted amino acid sequence obtained from the DNA sequence demonstrates a protein consisting of a heavy chain (Mr 35,400) linked to a light chain (Mr 27,600), both of which contain three sites for N-linked glycosylation. The light chain has clear homology with other serine proteinases, most notably in the region of the catalytically active and structurally important amino acids and shares some of the features characteristic of the plasminogen activators. The heavy chain has a clear ‘mosaic’ nature typical of the plasma serine proteinases; in particular it contains class A and class B LDL (low-density lipoprotein) receptor repeats with conserved cysteine residues similar to those found in other complement proteins.

Molecular Cloning of Bovine Amelogenin cDna

1987 ◽  
Vol 1 (2) ◽  
pp. 293-297 ◽  
Author(s):  
H. Shimokawa ◽  
Y. Ogata ◽  
S. Sasaki ◽  
M.E. Sobel ◽  
C.I. Mcquillan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Cloning ◽  
Peptide Sequence ◽  
Cdna Expression Library ◽  
Cdna Clones ◽  
Coding Region ◽  
Expression Library ◽  
Amino Acid Homology ◽  
Signal Peptide Sequence ◽  
Cloned Cdna

Molecular cloning of a bovine amelogenin cDNA was accomplished by construction of a cDNA expression library (λgt11 cDNA library) from the bovine ameloblast mRNA and then screening of the library with antibodies to bovine amelogenins. The complete primary structure of an amelogenin was deduced from cloned cDNA. One of the cDNA clones isolated from a bovine ameloblast phage λgt11 library had an 864-base-pair-long insert that encoded a protein with 216 amino acid residues. This cDNA clone appears to represent the complete coding region of amelogenin mRNA, including a putative AUG initiation codon and a signal peptide sequence. The predicted bovine amelogenin sequence has 87% amino acid homology with murine amelogenin.

scholarly journals The amino acid sequences of the myelin-associated glycoproteins: homology to the immunoglobulin gene superfamily

1987 ◽  
Vol 104 (4) ◽  
pp. 957-965 ◽  
Author(s):  
JL Salzer ◽  
WP Holmes ◽  
DR Colman
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Growth Factor Receptor ◽  
Amino Acid Sequences ◽  
Cdna Clones ◽  
Immunoglobulin Gene ◽  
Expression Library ◽  
Extracellular Region ◽  
Immunoglobulin Gene Superfamily ◽  
Membrane Spanning

The myelin associated glycoproteins (MAG) are integral plasma membrane proteins which are found in oligodendrocytes and Schwann cells and are believed to mediate the axonal-glial interactions of myelination. In this paper we demonstrate the existence in central nervous system myelin of two MAG polypeptides with Mrs of 67,000 and 72,000 that we have designated small MAG (S-MAG) and large MAG (L-MAG), respectively. The complete amino acid sequence of L-MAG and a partial amino acid sequence of S-MAG have been deduced from the nucleotide sequences of corresponding cDNA clones isolated from a lambda gt11 rat brain expression library. Based on their amino acid sequences, we predict that both proteins have an identical membrane spanning segment and a large extracellular domain. The putative extracellular region contains an Arg-Gly-Asp sequence that may be involved in the interaction of these proteins with the axon. The extracellular portion of L-MAG also contains five segments of internal homology that resemble immunoglobulin domains, and are strikingly homologous to similar domains of the neural cell adhesion molecule and other members of the immunoglobulin gene superfamily. In addition, the two MAG proteins differ in the extent of their cytoplasmically disposed segments and appear to be the products of alternatively spliced mRNAs. Of considerable interest is the finding that the cytoplasmic domain of L-MAG, but not of S-MAG, contains an amino acid sequence that resembles the autophosphorylation site of the epidermal growth factor receptor.

scholarly journals Human myeloperoxidase gene: molecular cloning and expression in leukemic cells

Blood ◽  
1986 ◽  
Vol 68 (6) ◽  
pp. 1411-1414 ◽  
Author(s):  
KS Chang ◽  
JM Trujillo ◽  
RG Cook ◽  
SA Stass
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Clone ◽  
Northern Blot ◽  
Single Gene ◽  
Myelogenous Leukemia ◽  
Cloning And Expression ◽  
Leukemic Cells ◽  
Expression Library

Abstract We have molecularly cloned the human myeloperoxidase (MPO) gene from the lambda gt11 expression library by screening with an affinity- purified MPO antibody. The cDNA clone of the MPO gene was used to study MPO gene expression in leukemic cells. The amino acid sequence predicted from the nucleotide sequence of the cDNA clone pMP401 matched exactly the 23 amino acid sequence of the NH2-terminal of the 60,000 MPO subunit. We found that MPO cDNA hybridized to a single EcoRI genomic band of 19 kb, indicating that the MPO gene represents a single gene in the human genome. Northern blot analysis of RNA isolated from leukemic cell lines and acute myelogenous leukemia (AML) patients' samples shows that MPO gene expression correlated with myeloid lineage. The intensity of MPO mRNA expression on Northern blot correlated with the level of MPO expression by cytochemical staining. Multiple species of MPO mRNA were found. This indicates that a single MPO gene may encode different RNA species through a mechanism of posttranscriptional processing or that multiple transcriptional start/termination sites exist in the MPO gene.

scholarly journals Amino acid sequence of the light chain of bovine protein C.

1982 ◽  
Vol 257 (20) ◽  
pp. 12170-12179 ◽  
Author(s):  
P Fernlund ◽  
J Stenflo
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Protein C
Sign in / Sign up

Export Citation Format

Share Document