Nucleotide sequence of cDNA clones encoding the complete precursor for subunit delta of thylakoid-located ATP synthase from spinach

1988 ◽  
Vol 10 (4) ◽  
pp. 323-330 ◽  
Author(s):  
J. Hermans ◽  
Ch. Rother ◽  
J. Bichler ◽  
J. Steppuhn ◽  
R. G. Herrmann
Keyword(s):  
Nucleotide Sequence ◽  
Atp Synthase ◽  
Cdna Clones

Construction and Identification by Partial Nucleotide Sequence Analysis of Bovine Casein and β-Lactoglobulin cDNA Clones

DNA ◽  
1982 ◽  
Vol 1 (4) ◽  
pp. 375-386 ◽  
Author(s):  
I.M. WILLIS ◽  
A.F. STEWART ◽  
A. CAPUTO ◽  
A.R. THOMPSON ◽  
A.G. MACKINLAY
Keyword(s):  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Nucleotide Sequence Analysis ◽  
Cdna Clones ◽  
Partial Nucleotide Sequence ◽  
Β Lactoglobulin

Mouse protamine 2 is synthesized as a precursor whereas mouse protamine 1 is not

1987 ◽  
Vol 7 (6) ◽  
pp. 2173-2179
Author(s):  
P C Yelick ◽  
R Balhorn ◽  
P A Johnson ◽  
M Corzett ◽  
J A Mazrimas ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Nucleotide Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Nucleotide Sequence Analysis ◽  
Cdna Clones ◽  
Protamine 1 ◽  
Protamine 2

The nuclei of mouse spermatozoa contain two protamine variants, mouse protamine 1 (mP1) and mouse protamine 2 (mP2). The amino acid sequence predicted from mP1 cDNAs demonstrates that mP1 is a 50-amino-acid protein with strong homology to other mammalian P1 protamines. Nucleotide sequence analysis of independently isolated, overlapping cDNA clones indicated that mP2 is initially synthesized as a precursor protein which is subsequently processed into the spermatozoan form of mP2. The existence of the mP2 precursor was confirmed by amino acid composition and sequence analysis of the largest of a set of four basic proteins isolated from late-step spermatids whose synthesis is coincident with that of mP1. The sequence of the first 10 amino acids of this protein, mP2 precursor 1, exactly matches that predicted from the nucleotide sequence of cDNA and genomic mP2 clones. The amino acid composition of isolated mP2 precursor 1 very closely matches that predicted from the mP2 cDNA nucleotide sequence. Sequence analysis of the amino terminus of isolated mature mP2 identified the final processing point within the mP2 precursor. These studies demonstrated that mP2 is synthesized as a precursor containing 106 amino acids which is processed into the mature, 63-amino-acid form found in spermatozoa.

Primary structure and microtubule-interacting domain of the SP-H antigen: a mitotic MAP located at the spindle pole and characterized as a homologous protein to NuMA

1993 ◽  
Vol 105 (2) ◽  
pp. 589-600 ◽  
Author(s):  
T. Maekawa ◽  
R. Kuriyama
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Functional Organization ◽  
Spindle Pole ◽  
Predicted Amino Acid Sequence ◽  
Cdna Clones ◽  
Globular Domain ◽  
Calculated Molecular Mass ◽  
Mammalian Cell Lines ◽  
Cell Biol

Using a human autoantibody, SP-H, we identified a 200–230 kDa mitotic MAP in a variety of mammalian cell lines which shows affinity for the minus end of microtubules and also becomes associated with the spindle pole during mitosis. To examine the detailed structure and functional organization of the protein, the gene coding for the end-specific MAP was isolated and characterized by screening a human placenta lambda gt11 expression library using SP-H as a probe. Overlapping cDNA clones, which covered the entire length of the coding region of the SP-H antigen, were obtained. Polyclonal antibodies raised against fusion proteins generated from non-overlapping cDNA fragments stained the HeLa SP-H antigen in interphase and mitotic cells, and recognized a single 215 kDa band on immunoblots, as did the original SP-H antibody. Analysis of the nucleotide sequence revealed a 7,091 nucleotide sequence with an open reading frame of 6,345 nucleotides encoding a 2,115 amino acid polypeptide with a calculated molecular mass of 238,376 Da. The predicted amino acid sequence showed the protein to be composed of an alpha-helical domain, flanked by globular domains located at the amino and carboxy termini. The sequence contained five repeats of the hypothetical leucine zipper motif: one is in the N-terminal globular domain, and four are in the central alpha-helical stalk. Comparison with other sequences in the database shows that the SP-H antigen is identical to the NuMA protein reported by Yang et al. (1992) J. Cell Biol. 116, 1303–1317, but there are differences between the SP-H antigen and NuMA sequence reported by Compton et al. (1992) J. Cell Biol. 116, 1395–1408. cDNA inserts of the truncated SP-H antigen were expressed in both insect Sf9 cells and in cultured mammalian cells. The recombinant protein corresponding to the C-terminal half of the protein was restricted to the nucleus, whereas the N-terminal half of the protein was localized in the cytoplasm, suggesting the presence of a nuclear translocation signal(s) in the C-terminal domain. The C-terminal polypeptide expressed in mitotic COS cells was shown to specifically localize at the spindle pole. Microtubule-binding assays using in vitro transcribed/translated polypeptide products from different domains of the SP-H antigen further suggested that the SP-H antigen interacts with microtubules through the globular domain at the C-terminus.

scholarly journals Complete Nucleotide Sequence and Genome Organization of Hibiscus Chlorotic Ringspot Virus, a New Member of the Genus Carmovirus: Evidence for the Presence and Expression of Two Novel Open Reading Frames

2000 ◽  
Vol 74 (7) ◽  
pp. 3149-3155 ◽  
Author(s):  
Mei Huang ◽  
Dora Chin-Yen Koh ◽  
Li-Juan Weng ◽  
Min-Li Chang ◽  
Yun-Kiam Yap ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Genome Organization ◽  
Complete Nucleotide Sequence ◽  
Full Length ◽  
Open Reading Frames ◽  
Ringspot Virus ◽  
In Vitro Translation ◽  
Cdna Clones ◽  
High Amino Acid ◽  
Reading Frames

ABSTRACT The complete nucleotide sequence of hibiscus chlorotic ringspot virus (HCRSV) was determined. The genomic RNA (gRNA) is 3,911 nucleotides long and has the potential to encode seven viral proteins in the order of 28 (p28), 23 (p23), 81 (p81), 8 (p8), 9 (p9), 38 (p38), and 25 (p25) kDa. Excluding two unique open reading frames (ORFs) encoding p23 and p25, the ORFs encode proteins with high amino acid similarity to those of carmoviruses. In addition to gRNA, two 3′-coterminated subgenomic RNA (sgRNA) species were identified. Full-length cDNA clones derived from gRNA and sgRNA were constructed under the control of a T7 promoter. Both capped and uncapped transcripts derived from the full-length genomic cDNA clone were infectious. In vitro translation and mutagenesis assays confirmed that all the predicted ORFs except the ORF encoding p8 are translatable, and the two novel ORFs (those encoding p23 and p25) may be functionally indispensable for the viral infection cycle. Based on virion morphology and genome organization, we propose that HCRSV be classified as a new member of the genus Carmovirus in familyTombusviridae.

scholarly journals Phenotypic expression in Escherichia coli and nucleotide sequence of two Chinese hamster lung cell cDNAs encoding different dihydrofolate reductases.

1984 ◽  
Vol 4 (1) ◽  
pp. 38-48 ◽  
Author(s):  
P W Melera ◽  
J P Davide ◽  
C A Hession ◽  
K W Scotto
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Nucleotide Sequence ◽  
Dihydrofolate Reductase ◽  
Phenotypic Expression ◽  
Chinese Hamster ◽  
Differential Sensitivity ◽  
Nucleotide Sequence Analysis ◽  
Cdna Clones ◽  
Weight Class

Nucleotide sequence analysis of two cDNA clones, one shown to direct the synthesis in Escherichia coli of the pI 6.7 form of the 20,000-molecular-weight class of Chinese hamster lung cell dihydrofolate reductase, and the other shown to direct the synthesis of the pI 6.5 form of the 21,000-molecular-weight class of the enzyme, has revealed the following: (i) the differences in physical and enzymatic properties displayed by these two proteins are due to two variations in their respective amino acid sequences with the conversion of Leu to Phe at position 22 probably responsible for the differential sensitivity of these two enzymes to methotrexate and methasquin; (ii) the multiple mRNAs responsible for the synthesis of each of these proteins differ in size due, at least in part, to a length heterogeneity at their 3' ends; (iii) these two proteins are encoded by different genes; and (iv) the sequence AAATATA appears to be a major polyadenylation signal in one Chinese hamster lung cell dihydrofolate reductase gene and a minor signal in another.

scholarly journals Nucleotide sequence of cDNA clones of the murine myb proto-oncogene.

1985 ◽  
Vol 4 (8) ◽  
pp. 2003-2008 ◽  
Author(s):  
T.J. Gonda ◽  
N.M. Gough ◽  
A.R. Dunn ◽  
J. de Blaquiere
Keyword(s):  
Nucleotide Sequence ◽  
Cdna Clones
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