scholarly journals The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins.

1984 ◽  
Vol 81 (18) ◽  
pp. 5709-5713 ◽  
Author(s):  
P. M. Steinert ◽  
D. A. Parry ◽  
E. L. Racoosin ◽  
W. W. Idler ◽  
A. C. Steven ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type I ◽  
Type Ii

scholarly journals The amino acid sequence of component 7c, a type II intermediate-filament protein from wool

1989 ◽  
Vol 261 (3) ◽  
pp. 1015-1022 ◽  
Author(s):  
L G Sparrow ◽  
C P Robinson ◽  
D T W McMahon ◽  
M R Rubira
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
British Library ◽  
Intermediate Filament Protein ◽  
Type I ◽  
Type Ii ◽  
Blocking Group ◽  
Intermediate Filament Proteins

Component 7c is one of the four homologous type II intermediate-filament proteins that, by association with the complementary type I proteins, form the microfibrils or intermediate filaments in wool. Component 7c was isolated as the S-carboxymethyl derivative from Merino wool and its amino acid sequence was determined by manual and automatic sequencing of peptides produced by chemical and enzymic cleavage reactions. It is an N-terminally blocked molecule of 491 residues and Mr (not including the blocking group) of 55,600; the nature of the blocking group has not been determined. The predicted secondary structure shows that component 7c conforms to the now accepted pattern for intermediate-filament proteins in having a central rod-like region of approximately 310 residues of coiled-coil alpha-helix flanked by non-helical N-and C-terminal regions. The central region is divided by three non-coiled-coil linking segments into four helical segments 1A, 1B, 2A and 2B. The N-and C-terminal non-helical segments are 109 and 71 residues respectively and are rich in cysteine. Details of procedures use in determining the sequence of component 7c have been deposited as a Supplementary Publication SUP 50152 (65 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1989) 257,5. The information comprises: (1) details of chemical and enzymic methods used for cleavage of component 7c, peptides CN1, CN2 and CN3, and various other peptides, (2) details of the procedures used for the fractionation and purification of peptides from (1), including Figures showing the elution profiles from the chromatographic steps used, (3) details of methods used to determine the C-terminal sequence of peptide CN3, and (4) detailed evidence to justify a number of corrections to the previously published sequence.

scholarly journals Composition and Diversity of CRISPR-Cas13a systems in the genus Leptotrichia

2019 ◽  
Author(s):  
Shinya Watanabe ◽  
Bintao Cui ◽  
Kotaro Kiga ◽  
Yoshifumi Aiba ◽  
Xin-Ee Tan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Host Cell ◽  
Type I ◽  
Whole Genome ◽  
Type Ii ◽  
Genome Sequences ◽  
Type Iv ◽  
Rna Targeting ◽  
Sequence Similarities

AbstractClustered regularly interspaced short palindromic repeats (CRISPR)-Cas13a, previously known as CRISPR-C2c2, is the most recently identified RNA-guided RNA-targeting CRISPR-Cas system and has the unique characteristics of both targeted and collateral single-stranded RNA (ssRNA) cleavage activities, which was first identified in Leptotrichia shahii CRISPR-Cas13a. Here, the complete whole genome sequences of 11 Leptotrichia strains were determined and compared with 18 publicly available Leptotrichia genomes in regard to the composition, occurrence and diversity of the CRISPR-Cas13a and other CRISPR-Cas systems. Various types of CRISPR-Cas systems, I-B, II-C, III-A, III-D, III-like and VI-A, were unevenly distributed among the Leptotrichia genomes, accounting for 10 (34.4%), 1 (2.6%), 6 (15.4%), 6 (15.4%), 3 (7.7%) and 11 (37.9%) of the 29 strains, respectively, while 8 (20.5%) strains had no CRISPR-Cas system. The Cas13a effectors were highly divergent with amino acid sequence similarities ranging from 61% to 90% to that of L. shahii and their collateral ssRNA cleavage activities, resulting in cytotoxicity to host cell, were found to be maintained. CRISPR-Cas spacers represent a sequential achievement of former intruder encounters, and the retained spacers reflect the evolutionary phylogeny or relatedness of strains. Analysis of spacer contents and numbers among Leptotrichia species showed considerable diversity with only 2 (0.5%) of 400 spacers through CRIPSR-Cas I-VI were shared by two strains. The organisation and distribution of CRISPR-Cas systems (type I-VI) encoded by all registered Leptotrichia species revealed that effector or spacer sequences of the CRISPR-Cas systems were very divergent, and the prevalence of types I, III and VI was almost equal. There was only one strain carrying type II, while none carried type IV or V. These results provide new insights into the characteristics and divergences of CRISPR-Cas systems among Leptotrichia species.

scholarly journals Isolation and Characterization of a Type I Gene Encoding a Light-harvesting Chlorophyll a/b-binding Protein of Photosystem II in Peach

1998 ◽  
Vol 123 (4) ◽  
pp. 493-499 ◽  
Author(s):  
Kyu H. Chung ◽  
Dennis E. Buetow ◽  
Schuyler S. Korban
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Photosystem Ii ◽  
Amino Acid Sequence ◽  
Woody Plants ◽  
Light Harvesting ◽  
Binding Protein ◽  
Transit Peptide ◽  
Type I ◽  
Polyadenylation Sites

A nuclear gene, Lhcb1*Pp1, encoding a light-harvesting chlorophyll a/b-binding protein of photosystem II has been isolated from peach [Prunus persica (L.) Batsch. `Stark Earliglo'] leaf genomic DNA, cloned, and sequenced. This gene encodes a precursor polypeptide of 267 amino acids with a transit peptide of 34 and a type I mature protein of 233 amino acids. The amino acid sequence of the mature polypeptide is 89% to 94% and 80% to 94% similar to those encoded by type I Lhcb genes of annual and other woody plants, respectively. In contrast, the amino acid sequence of the peach transit peptide is less conserved being 47% to 69% similar to those of annual plants and only 17% to 22% similar to those of other woody plants. The peach gene was used as a probe for Lhcb gene expression. Lhcb mRNA is detected in leaves of field-grown trees during June to October. Lhcb mRNA is detected at a high level in leaves of peach shoots grown in tissue culture in the light, but only at a trace level in leaves grown in the dark. Some Lhcb genes appear to be light-modulated in stems. Lhcb1*Ppl contains four potential polyadenylation sites. S1 nuclease analysis detected transcripts of the sizes expected from each of the four polyadenylation sites. All four are found in leaves of light-grown shoots and of field-grown trees throughout the growing season. In contrast, only three are detected in stems of light-grown shoots.

scholarly journals Seven new mutations in the nicotinamide adenine dinucleotide reduced–cytochrome b5 reductase gene leading to methemoglobinemia type I

Blood ◽  
2001 ◽  
Vol 97 (4) ◽  
pp. 1106-1114 ◽  
Author(s):  
Jan Dekker ◽  
Michel H. M. Eppink ◽  
Rob van Zwieten ◽  
Thea de Rijk ◽  
Angel F. Remacha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Cytochrome B5 ◽  
Enzyme Inactivation ◽  
Amino Acid Substitutions ◽  
Type I ◽  
Type Ii ◽  
3 Dimensional ◽  
Cytochrome B5 Reductase ◽  
Fad Binding

Abstract Cytochrome b5 reductase (b5R) deficiency manifests itself in 2 distinct ways. In methemoglobinemia type I, the patients only suffer from cyanosis, whereas in type II, the patients suffer in addition from severe mental retardation and neurologic impairment. Biochemical data indicate that this may be due to a difference in mutations, causing enzyme instability in type I and complete enzyme deficiency or enzyme inactivation in type II. We have investigated 7 families with methemoglobulinemia type I and found 7 novel mutations in the b5R gene. Six of these mutations predicted amino acid substitutions at sites not involved in reduced nicotinamide adenine dinucleotide (NADH) or flavin adenine dinucleotide (FAD) binding, as deduced from a 3-dimensional model of human b5R. This model was constructed from comparison with the known 3-dimensional structure of pig b5R. The seventh mutation was a splice site mutation leading to skipping of exon 5 in messenger RNA, present in heterozygous form in a patient together with a missense mutation on the other allele. Eight other amino acid substitutions, previously described to cause methemoglobinemia type I, were also situated in nonessential regions of the enzyme. In contrast, 2 other substitutions, known to cause the type II form of the disease, were found to directly affect the consensus FAD-binding site or indirectly influence NADH binding. Thus, these data support the idea that enzyme inactivation is a cause of the type II disease, whereas enzyme instability may lead to the type I form.

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3',5'-phosphate-dependent protein kinase

Biochemistry ◽  
1983 ◽  
Vol 22 (15) ◽  
pp. 3702-3709 ◽  
Author(s):  
Shozo Shoji ◽  
Lowell H. Ericsson ◽  
Kenneth A. Walsh ◽  
Edmond H. Fischer ◽  
Koiti Titani
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Catalytic Subunit ◽  
Type Ii ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Bovine Type

scholarly journals Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization

1993 ◽  
Vol 290 (3) ◽  
pp. 873-884 ◽  
Author(s):  
H C Blair ◽  
S L Teitelbaum ◽  
L E Grosso ◽  
D L Lacey ◽  
H L Tan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Substrate Specificity ◽  
Cathepsin B ◽  
Type I Collagen ◽  
Sequence Similarity ◽  
Bone Matrix ◽  
Collagenolytic Activity ◽  
Type I ◽  
Isolation And Characterization

Osteoclasts degrade bone matrix, which is mainly type I collagen and hydroxyapatite, in an acidic extracellular compartment. Thus we reasoned that osteoclasts must produce an acid collagenase. We purified this enzyme, a 31 kDa protein, from avian osteoclast lysates (in 100 mM acetate/1 mM CHAPS/1 mM dithiothreitol, pH 4.4), fractionated by (NH2)2SO4 precipitation, gelatin-affinity, cation exchange, and gel filtration. Fraction activity was measured using diazotized collagen or 3H-labelled cross-linked collagen (decalcified and trypsin-treated metabolically L-[4,5-3H]proline-labelled bone) as substrates. Iodoacetate, leupeptin, antipain, pepstatin and mercurials inhibited collagenolysis by the isolated proteinase; mercurial derivatives could not be re-activated by dithiothreitol. Collagen degradation was maximal at pH 4.4; purified proteinase reproduced the collagenolytic activity of cell lysates. The N-terminal amino acid sequence from the isolated protein and its CNBr degradation fragments showed sequence similarity to mammalian cathepsin Bs, and near-identity with avian liver cathepsin B. Peptide substrate specificity of the osteoclastic enzyme resembled those of mammalian cathepsin B and its avian liver counterpart, but degradation of low-molecular-mass substrates by the osteoclastic enzyme was slower, reflecting generally lower kcat. values. Further, kcat/Km varied less between arginine-containing substrates than for previously reported cathepsin Bs, indicating different substrate specificity of the osteoclast enzyme. Polyclonal antibody raised to a 25 kDa fragment of the enzyme recognized a single 31 kDa band in SDS/PAGE of osteoclast lysates blotted to poly(vinylidene difluoride), adsorbed collagenolytic activity of osteoclast lysates, and stained avian osteoclasts in tissue sections. Degenerate sense- and antisense-oligonucleotide primers, predicted from segments of primary amino acid sequence, amplified a 486 bp DNA fragment; this was cloned and sequenced. Of 162 amino acids encoded, 77% are identical with those of human cathepsin B; hybridization identified a 2.4 kb RNA in osteoclast lysates. We conclude that the major avian osteoclast collagenolytic enzyme is a cathepsin B, whose activity varies from other enzymes of its class.

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