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S Altman

Publications and source records attributed to S Altman.

At least 181 records · Page 10Linked to original sources
PubMed1976

Nucleotide sequence and in vitro processing of a precursor molecule to Escherichia coli 4.5 S RNA.

A precursor molecule to the stable 4.5 S RNA species of Escherichia coli has been found to accumulate at 42 degrees in a strain thermosensitive for the function of ribonuclease P. The precursor molecule is 130 nucleotides long. Twenty-two extra nucleotides, starting with pppGp, precede the mature sequence at its 5' terminus. At least 1 extra uridine residue can be found at the 3' terminus. The precursor to 4.5 S RNA is cleaved in vitro by RNase P to generate a 5' end identical to that of the mature 4.5 S RNA.

Base Sequence↗
PubMed1976

Identification of a ribonuclease P-like activity from human KB cells.

An endoribonuclease which cleaves tRNA precursor molecules has been partially purified from human KB tissue culture cells. This activity is found in cytoplasmic fractions but is not detectable in the nucleoplasm. tRNA precursor molecules from both E. coli and KB cells are cleaved by this novel activity to produce 5' phosphate-terminated oligonucleotides. E coli RNAase P and the KB cell nuclease both make a single endonucleolytic scission in E. coli tRNATyr precursor, thereby separating the 41 extra nucleotides on the 5' end of the precursor molecule from the 5' terminal sequence of the mature tRNATyr molecule. The cleavage products generated from other E. coli tRNA precursors by the KB cell activity are identical in size to those produced by RNAase P. The KB cell endoribonuclease requires Mg2+ and a monovalent cation (Na+, K+, or NH4+) for function. The enzymatic activity has a broad pH optimum, centered near pH 8.0, and the activity is inhibited by tRNA. Several KB cell RNAs with long half-lives in vivo, including 5S and bulk 4S RNA, are not cleaved by this nuclease. The KB cell endoribonuclease resembles E. coli RNAase P in its substrate specificity, pH optimum, ion requirements, and sensitivity to tRNA. These properties and the cytoplasmic localization of the novel endoribonuclease indicate its involvement in the biosynthesis of KB cell tRNA.

Ammonia↗
PubMed1976

Ribonuclease P substrate specificity: cleavage of a bacteriophage phi80-induced RNA.

RNase P can cleave in vitro a bacteriophage phi80-induced RNA which is 62 nucleotides long [M3 RNA, G. Pieczenik et al. (1972) Arch. Biochem. Biophys. 152, 152-165] to yield two specific fragments 25 and 37 nucleotides long. As is the case for another substrate of RNase P; the precursor to Escherichia coli 4.5S RNA, the cleavage site in M3 RNA is at the end of a long double-stranded region immediately adjacent to a single-stranded segment. Similar nucleotide sequences span the cleavage site in both substrates. These and other features of the reaction of RNase P with M3 and 4.5S precursor RNA are different from some aspects of the reaction of this enzyme with tRNA precursor molecules. A qualitative scheme is presented that is directed towards the understanding of the differences in RNase P cleavage site specificity for these substrates.

Binding Sites↗
PubMed1976

A modified uridine in the anticodon of E. coli tRNA I Tyr su + oc.

The anticodon of an ochre-suppressing derivative of E. coli tRNA I Tyr, previously identified as UUA, can contain a modified uridine (U+) in the first position. The novel modified nucleotide has been identified by two-dimensional thin layer chromatography following RNase T2 digestion of anticodon-containing fragments. Up+ is found in less than stoichiometric molar yields in preparations of tRNA I Tyr su + oc. The electrophoretic mobility of Up+ is the same as Up at pH 3.5 and pH 7.5. U+ probably does not contain sulfur since it cannot be labeled with 35S in vivo incorporation experiments.

Anticodon↗
PubMed1975

9-Aminoacridine mutagenesis of bacteriophage T4 intracellular DNA.

Most of the intracellular T4 DNA made in the presence of 9-aminoacridine is of lower molecular weight than mature T4 DNA and does not get packaged into phage particles. Using a T4 DNA transformation assay, we have examined this intracellular T4 DNA for its content of 9-aminoacridine-induced revertants of certain rII gene frameshift mutations. The proportion of acridine-induced revertants in the intracellular DNA population is close to that found in the phage progency made in the presence of 9-aminoacridine. Thus, the generation of low molecular weight T4 DNA in the presence of 9-aminoacridine is not, in itself, also a mutagenic process.

Acridines↗
PubMed1975

Partial purification and properties of an endoribonuclease isolated from human KB cells.

With the use of a precursor to Escherichia coli tRNA-Tyr as a substrate, we have detected and partially purified a novel endoribonuclease from the cytoplasm of human KB tissue culture cells. This activity, which we have called RNase NU, cleaves the tRNA precursor at two sites in that part of the molecule which is not included in the mature tRNA sequence and which is normally degraded in vivo. In keeping with this observation, we have found that, of a variety of substrates tested, only those which are unstable in vivo are attacked by RNase NU. RNase NU can be purified from the 0.2 M NH4Cl wash of ribosomes followed by ammonium sulfate fractionation and DEAE-Sephadex chromatography. RNase NU cleaves RNA to create 3'-phosphate-terminated oligonucleotides. It has a pH optimum near 8.0, requires either a monovalent cation (NH4+ is most efficient) or Ca-2+ for optimal activity, and is inhibited by 0.1 M PO4-3-. In the course of purifying RNase NU we have detected and studied the intracellular distribution of other ribonuclease activities in human KB cells.

Base Sequence↗
PubMed1975

Characterization of ribonuclease NU cleavage sites in a bacteriophage phi80-induced ribonucleic acid.

Ribonuclease NU, an endoribonuclease isolated from human KB tissue culture cells, can cleave a bacteriophage phi80-induced RNA at four distinct sites. Nucleotide sequence analysis of the eight cleavage products has shown that the enzyme produces oligonucleotides terminating in 3'-phosphate groups, and that the four cleavage sites are in the only nonhydrogen-bonded region of the substrate. Various aspects of the cleavage reaction with this RNA and with other substrates are discussed.

Base Sequence↗
PubMed1973

Nucleotide modification in vitro of the precursor of transfer RNA of Escherichia coli.

Certain nucleotides in precursor RNA of tRNA(Tyr) of Escherichia coli were modified in vitro with a preparation of partially purified E. coli enzyme containing ribothymidine- and pseudouridine-forming activity. The only nucleotides modified in vitro are the same as those found modified in mature tRNA. The best substrate for these modifying enzymes is the RNase P cleavage product of the precursor RNA, which contains the mature tRNA sequence. Of the two pseudouridines found in mature tRNA, one (in the TPsiC sequence) can be formed in intact precursor RNA. The other (in the anticodon stem) can only be formed in the cleaved precursor RNA. The presence of modified nucleotides in the precursor RNA does not enhance its rate of cleavage by RNase P.

Adenosine↗