Tissue-specific expression of mouse α-amylase genes: Nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland

Hagenbüchle, Otto; Bovey, R; Young, Richard A.

doi:10.1016/0092-8674(80)90125-7

Cited by 263 publications

(86 citation statements)

References 29 publications

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“…The most consistently observed sequence associated with polyadenylation sites is an AAUAAA located 11 to 30 nucleotides 5' of the poly(A) addition site (42); also noted but with lesser frequency is the sequence AUUAAA (8,21,26). In accord with this we observed that in the calcitonin/CGRP gene, the sequences AAUAAA and AUUAAA appeared to be the appropriate distances upstream of the polyadenylation sites for calcitonin and CGRP mRNAs, respectively.…”

Section: Discussionsupporting

confidence: 74%

Calcitonin/calcitonin gene-related peptide transcription unit: tissue-specific expression involves selective use of alternative polyadenylation sites.

Amara¹,

Evans²,

Rosenfeld³

1984

Mol. Cell. Biol.

199

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Different 3' coding exons in the rat calcitonin gene are used to generate distinct mRNAs encoding either the hormone calcitonin in thyroidal C-cells or a new neuropeptide referred to as calcitonin gene-related peptide in neuronal tissue, indicating the RNA processing regulation is one strategy used in tissue-specific regulation of gene expression in the brain. Although the two mRNAs use t-he same transcriptional initiation site and have identical 5' terminal sequences, their 3' termini are distinct. The polyadenylation sites for calcitonin and calcitonin gene-related peptide mRNAs are located at the end of the exons 4 and 6, respectively. Termination of transcription after the calcitonin exon does not dictate the production of calcitonin mRNA, because transcription proceeds through both c4lcitonin and calcitonin gene-related peptide exons irrespective of which mRNA is ultimately produced. In isolated nuclei, both polyadenylation sites appear to be utilized; however, the proximal (calcitonin) site is preferentially used in nuclei from tissues producing calcitonin mRNA. These data suggest that the mechanism dictating production of each mRNA involves the selective use of alternative polyadenylation sites.

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Section: Discussionsupporting

confidence: 74%

Calcitonin/calcitonin gene-related peptide transcription unit: tissue-specific expression involves selective use of alternative polyadenylation sites.

Amara¹,

Evans²,

Rosenfeld³

1984

Mol. Cell. Biol.

199

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“…No homology was apparent between the primary structures of Gl and or-amylases described in the literature (14,21,31,37,46,47). Three fungal carbohydrases, a mycodextranase (36), a cellobiohydrolase (9,13), and the glucoamylase G1 (34,44), which all attack insoluble substrates, i.e.…”

Section: Discussionmentioning

confidence: 99%

The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger

Svensson

Larsen

Svendsen

et al. 1983

Carlsberg Res. Commun.

188

158

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The primary structure ofglucoamylase G1 (EC 3.2.1.3) from Aspergillus niger has been determined. Fragments of GI were obtained by cleavage with either cyanogen bromide, hydroxylamine, or S. aureus V8 protease. The resulting peptides were separated using ion exchange chromatography on DEAE-Sephacel, gel filtration, and affinity chromatography on Con A-Sepharose. Secondary fragments were generated by cleavage with either o-iodosobenzoic acid or BNPS-skatole as well as by digestion with S. aureus V8 protease, trypsin, and endoproteinase Lys-C. These peptides were purified by the procedures mentioned above and by reverse phase HPLC. The present fragments were amino acid sequenced and this permitted, in combination with the tryptic peptides (Carlsberg Res. Commun. 48, 517-527 (1983)), identification of 574 of the 614 amino acid residues in Gl. Sequencing of glucoamylase Gl cDNA, constructed from A. niger total mRNA, enabled deduction of the sequence of the remaining 40 amino acid residues localized to 6 short stretches. From the alignment of the fragments the complete primary structure of the enzyme was established. The amino acid sequence corresponds to a molecular weight of the polypeptide moiety of 65,424. Including both hexosamine and neutral carbohydrate contents the molecular weight of the present sample of G1 was calculated to be about 82,000.The majority of the carbohydrate of Gl is found in a highly glycosylated region of 70 amino acid residues which comprises about 35 O-glycosyl serine and threonine residues. This region ends approximately 100 residues from the C-terminus of the enzyme. Two N-glycosylated positions were found in the central part of the polypeptide chain. The molecule contains 9 half-cystine residues. No homology is apparent between the sequence of glycoamylase and various at-amylases.Abbreviations: BNPS-skatole = 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine; ca = citraconyl; Con A = concanavalin A; DFP = diisopropylfluorophosphate; DPCC = diphenylcarbamyl chloride; EDTA = ethylenediaminetetraacetic acid, disodium salt; Hepes = N-2-hydroxyethyl piperazine-N'-2-ethanesulfonic acid; Nemac = N-ethylmorpholine acetate; HPLC = high pressure liquid chromatography; PTH = phenylthiohydantoin; SDS-PAGE = polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate; 2-pe = 2-pyridylethyl; G I designates the larger and G2 the smaller of the forms ofglucoamylase from A. niger (44).

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“…Although there is no general sequence homology between this glucoamylase and known ttamylases (10,18,24,32,33), it was observed that a short stretch of polypeptide chain, preceding Trp(120) in glucoamylase and the Trp(83) in the Taka-amylase A (20) (from A. oryzae) was identical ( Figure 5). The Trp(83) is located in the active site cleft of the three-dimensional structure ofTaka-amylase A and model fitting studies with amylose have recently proposed that Trp(83) participates in binding of this substrate (20).…”

Section: Discussionmentioning

confidence: 99%

Identification of an essential tryptophanyl residue in the primary structure of glucoamylase G2 from aspergillus niger

Clarke

Svensson

1984

Carlsberg Res. Commun.

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Enzymatically active, N-bromosuccinimide oxidized glucoamylase G2 (EC 3.2.1.3) was prepared in the presence of the inhibitor acarbose and inactive, oxidized G2 with capacity to bind substrate was prepared in the presence of maltose. Four out of 15 tryptophanyl residues were oxidized in the first derivative and five in the latter. In order to identify this fifth and essential residue, tryptie fragments of the two G2 derivatives were isolated. The peptide fragment from the inactive G2 der/vative containing the additional oxindolealaniae residue was Tocated in HPLC chromatograms by UV-absorption measurements. Normal and second derivative UV-spectra, amino acid composition and NH_,-terminal sequence of the isolated fragment led to identification of Trp(120) as a residue essential for activity. A short homologous amino acid sequence precedes both this Trp(120) and the Trp(83) which is involved in substrate binding in Taka-amylase A (J. Biochem. 95, 697-702 (1984)).

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Tissue-specific expression of mouse α-amylase genes: Nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland

Cited by 263 publications

References 29 publications

Calcitonin/calcitonin gene-related peptide transcription unit: tissue-specific expression involves selective use of alternative polyadenylation sites.

Calcitonin/calcitonin gene-related peptide transcription unit: tissue-specific expression involves selective use of alternative polyadenylation sites.

The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger

Identification of an essential tryptophanyl residue in the primary structure of glucoamylase G2 from aspergillus niger

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