Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence

Biochemistry ◽  
1990 ◽  
Vol 29 (20) ◽  
pp. 4863-4870 ◽  
Author(s):  
Philip C. Trackman ◽  
Ann Marie Pratt ◽  
Andrzej Wolanski ◽  
Shiow Shih Tang ◽  
Gwynneth D. Offner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lysyl Oxidase ◽  
Rat Aorta ◽  
Predicted Amino Acid Sequence

Cloning of rat aorta lysyl oxidase cDNA: complete codons and predicted amino acid sequence [Erratum to document cited in CA112(25):230629x]

Biochemistry ◽  
1991 ◽  
Vol 30 (33) ◽  
pp. 8282-8282 ◽  
Author(s):  
Philip C. Trackman ◽  
Ann Marie Pratt ◽  
Andrzej Wolanski ◽  
Shiow Shih Tang ◽  
Gwynneth D. Offner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lysyl Oxidase ◽  
Rat Aorta ◽  
Predicted Amino Acid Sequence

Conserved DNA binding and self-association domains of the Drosophila zeste protein

1992 ◽  
Vol 12 (2) ◽  
pp. 598-608
Author(s):  
J D Chen ◽  
C S Chan ◽  
V Pirrotta
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Coiled Coil ◽  
Helical Structure ◽  
Binding Activity ◽  
Binding Domain ◽  
Drosophila Virilis ◽  
Predicted Amino Acid Sequence ◽  
Dna Binding Domain

The zeste gene product is involved in two types of genetic effects dependent on chromosome pairing: transvection and the zeste-white interaction. Comparison of the predicted amino acid sequence with that of the Drosophila virilis gene shows that several blocks of amino acid sequence have been very highly conserved. One of these regions corresponds to the DNA binding domain. Site-directed mutations in this region indicate that a sequence resembling that of the homeodomain DNA recognition helix is essential for DNA binding activity. The integrity of an amphipathic helical region is also essential for binding activity and is likely to be responsible for dimerization of the DNA binding domain. Another very strongly conserved domain of zeste is the C-terminal region, predicted to form a long helical structure with two sets of heptad repeats that constitute two long hydrophobic ridges at opposite ends and on opposite faces of the helix. We show that this domain is responsible for the extensive aggregation properties of zeste that are required for its role in transvection phenomena. A model is proposed according to which the hydrophobic ridges induce the formation of open-ended coiled-coil structures holding together many hundreds of zeste molecules and possibly anchoring these complexes to other nuclear structures.

scholarly journals Conserved DNA binding and self-association domains of the Drosophila zeste protein.

1992 ◽  
Vol 12 (2) ◽  
pp. 598-608 ◽  
Author(s):  
J D Chen ◽  
C S Chan ◽  
V Pirrotta
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Coiled Coil ◽  
Helical Structure ◽  
Binding Activity ◽  
Binding Domain ◽  
Drosophila Virilis ◽  
Predicted Amino Acid Sequence ◽  
Dna Binding Domain

The zeste gene product is involved in two types of genetic effects dependent on chromosome pairing: transvection and the zeste-white interaction. Comparison of the predicted amino acid sequence with that of the Drosophila virilis gene shows that several blocks of amino acid sequence have been very highly conserved. One of these regions corresponds to the DNA binding domain. Site-directed mutations in this region indicate that a sequence resembling that of the homeodomain DNA recognition helix is essential for DNA binding activity. The integrity of an amphipathic helical region is also essential for binding activity and is likely to be responsible for dimerization of the DNA binding domain. Another very strongly conserved domain of zeste is the C-terminal region, predicted to form a long helical structure with two sets of heptad repeats that constitute two long hydrophobic ridges at opposite ends and on opposite faces of the helix. We show that this domain is responsible for the extensive aggregation properties of zeste that are required for its role in transvection phenomena. A model is proposed according to which the hydrophobic ridges induce the formation of open-ended coiled-coil structures holding together many hundreds of zeste molecules and possibly anchoring these complexes to other nuclear structures.

The Complete Derived Amino Acid Sequence of Human Lysyl Oxidase and Assignment of the Gene to Chromosomes 5

Matrix ◽  
1992 ◽  
Vol 12 (3) ◽  
pp. 242-248 ◽  
Author(s):  
Thomas J. Mariani ◽  
Philip C. Trackman ◽  
Herbert M. Kagan ◽  
Roger L. Eddy ◽  
Thomas B. Shows ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lysyl Oxidase

scholarly journals Cloning, expression and map assignment of chicken prosaposin

1998 ◽  
Vol 330 (1) ◽  
pp. 321-327 ◽  
Author(s):  
Norihiro AZUMA ◽  
Hee-Chan SEO ◽  
Øystein LIE ◽  
Qiang FU ◽  
M. Robert GOULD ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mammalian Species ◽  
Three Dimensional ◽  
Glycosylation Site ◽  
Amino Acid Sequences ◽  
Predicted Amino Acid Sequence ◽  
Chicken Brain ◽  
Saposin C ◽  
Saposin B

Prosaposin is the precursor of four small glycoproteins, saposins A-D, that activate lysosomal sphingolipid hydrolysis. A full-length cDNA encoding prosaposin from chicken brain was isolated by PCR. The deduced amino acid sequence predicted that, similarly to human and other mammalian species studied, chicken prosaposin contains 518 residues, including four domains that correspond to saposins A-D. There was 59% identity and 76% similarity of human and chicken prosaposin amino acid sequences. The basic three-dimensional structures of these saposins is predicted to be similar on the basis of the conservation of six cysteine residues and an N-glycosylation site. Identity of amino acid sequences was higher among saposins A, B and D than in saposin C. The predicted amino acid sequence of saposin B matched exactly that of purified chicken saposin B protein. The chicken prosaposin gene was mapped to a single locus, PSAP, in chicken linkage group E11C10 and is closely linked to the ACTA2 locus. This confirms the homology between chicken and human prosaposins and defines a new conserved segment with human chromosome 10q21-q24.

Sequence and expression of a stem-abundant caffeic acid O-methyltransferase cDNA from perennial ryegrass (Lolium perenne)

1998 ◽  
Vol 25 (2) ◽  
pp. 225 ◽  
Author(s):  
Fiona M. McAlister ◽  
Colin L. D. Jenkins ◽  
John M. Watson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Caffeic Acid ◽  
Lolium Perenne ◽  
Perennial Ryegrass ◽  
Leaf Sheath ◽  
Predicted Amino Acid Sequence ◽  
Degenerate Oligonucleotide ◽  
Blot Hybridisation ◽  
Southern Blot Hybridisation

A perennial ryegrass (Lolium perenne) cDNA library was screened with a PCR-amplified comt DNA fragment generated from ryegrass cDNA template using degenerate oligonucleotide primers. A full-length cDNA (LpeComt1) was isolated and shown to encode a caffeic acid O-methyltransferase (COMT) enzyme by analysis of its predicted amino acid sequence. This cDNA was expressed in E.coli and COMT activity was demonstrated in bacterial extracts. The predicted amino acid sequence of the perennial ryegrass COMT was highly similar (88%) with that of a COMT isolated from maize. Southern blot hybridisation analysis using this cDNA indicated that it is a member of a small gene family comprising at least two genes in perennial ryegrass. The LpeComt1 gene is strongly expressed in stem tissue, but not obviously in shoot, leaf blade, leaf sheath, flower or root tissue.

Target site–based penoxsulam resistance in barnyardgrass (Echinochloa crus-galli) from China

Weed Science ◽  
2019 ◽  
Vol 67 (3) ◽  
pp. 281-287 ◽  
Author(s):  
Jiapeng Fang ◽  
Tingting Liu ◽  
Yuhua Zhang ◽  
Jun Li ◽  
Liyao Dong
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
Predicted Amino Acid Sequence ◽  
Sequence Analyses ◽  
Als Inhibitors ◽  
Higher Sensitivity

AbstractBarnyardgrass [Echinochloa crus-galli (L.) P. Beauv.] is acknowledged to be the most troublesome weed in rice fields in Anhui and Jiangsu provinces of China. It cannot be effectively controlled using certain acetolactate synthase (ALS)-inhibiting herbicides, including penoxsulam. Echinochloa crus-galli samples with suspected resistance to penoxsulam were collected to identify the target site–based mechanism underlying this resistance. Populations AXXZ-2 and JNRG-2 showed 33- and 7.3-fold resistance to penoxsulam, respectively, compared with the susceptible JLGY-3 population. Cross-resistance to other ALS inhibitors was reported in AXXZ-2 but not in JNRG-2, and occasionally showed higher sensitivity than JLGY-3. In vitro ALS activity assays revealed that penoxsulam concentrations required to inhibit 50% of ALS activity were 11 and 5.2 times greater in AXXZ-2 and JNRG-2, respectively, than in JLGY-3. DNA and predicted amino acid sequence analyses of ALS revealed Ala-205-Val and Ala-122-Gly substitutions in AXXZ-2 and JNRG-2, respectively. Our results indicate that these substitutions in ALS are at least partially responsible for resistance to penoxsulam.

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