Genes for Bacillus megaterium small, acid-soluble spore proteins: nucleotide sequence of two genes and their expression during sporulation

Fliss, E R; Setlow, Peter

doi:10.1016/0378-1119(85)90167-2

Cited by 22 publications

(20 citation statements)

References 13 publications

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“…Thus, genes for four different SASP closely related to SASP-A have been cloned and sequenced to date. One gene is that for SASP-C (3,6), one is for SASP-C-3, a minor spore protein immunologically related to SASP-A and -C (2, 7), and the other two (SASP-C-1 and -C-2 genes) are almost identical in their coding sequence and code for proteins extremely similar in sequence to SASP-A and -C (8). All these genes (as well as the SASP-A gene) are expressed in parallel during sporulation but only within the developing forespore, and SASP synthesis is regulated at the transcriptional level (5,8).…”

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Genes for Bacillus megaterium small, acid-soluble spore proteins: cloning and nucleotide sequence of three additional genes from this multigene family

Fliss¹,

Loshon²,

Setlow³

1986

J Bacteriol

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Three genes coding for small, acid-soluble spore proteins (SASP) were cloned from Bacillus megaterium, using previously cloned B. megaterium SASP genes (SASP-C and -C-3) as DNA-DNA hybridization probes. One gene (SASP-A) codes for the A protein, a previously identified major SASP. The other two (termed genes for SASP-C-4 and -C-5) are extremely similar in much of their nucleotide sequence to the previously cloned B. megaterium SASP-C-2 gene. The proteins coded for by all these SASP genes had extensive sequence homology with each other and with those coded for by the B. megaterium SASP-C, -C-1, -C-2, and -C-3 genes. Their coding sequences are preceded by strong ribosome-binding sites and are followed by regions of dyad symmetry which presumably are transcription stop sites. The SASP-A, -C-4, and -C-5 genes are expressed in parallel during sporulation, and their transcription start points were localized by the size of the mRNAs produced. The sequences localized 10 and 35 base pairs upstream from the transcription start points show significant homology with the analogous regions of the SASP-C, -C-1, -C-2, and -C-3 genes. The identification of seven closely related SASP genes in B. megaterium indicates that the SASP are the products of a very extensive multigene family.

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confidence: 99%

Genes for Bacillus megaterium small, acid-soluble spore proteins: cloning and nucleotide sequence of three additional genes from this multigene family

Fliss¹,

Loshon²,

Setlow³

1986

J Bacteriol

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“…They are soluble in dilute acid and their accumulation is regulated at the transcriptional level. All three proteins have low mol wt (7-10,000), basic pl (>9.8), alanine as the NH2-terminal amino acid, lack cysteine, cystine, and tryptophan, and appear to be encoded by a multigene family (12). A critical difference between these bacterial storage proteins and seed storage proteins is that these bacterial proteins are also capable of binding to nucleic acids (26).…”

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confidence: 99%

Biochemistry of Fern Spore Germination: Globulin Storage Proteins in Matteuccia struthiopteris L.

Templeman

DeMaggio²,

Stetler³

1987

Plant Physiol.

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Two globulin storage proteins have been identified in spores of the ostrich fern, Matteuccia struthiopteris (L.) Todaro. The two proteins comprise a significant amount of the total spore protein, are predominantly salt-soluble, and can be extracted by other solvents to a limited extent. The large 113 Svedberg unit (S) globulin is composed of five polypeptides with molecular weights of 21,000, 22,000, 24,000, 28,000 and 30,000. Each polypeptide has several isoelectric point (pI) variants between pH 5 and 7. The small 2.2S storage protein has a pI > 10.5 and is composed of at least two major polypeptides of 6,000 and 14,000 Mr. Some pertinent information concerning storage proteins in the spores of bacteria and algae is available. Bacteria contain storage proteins that accumulate in large quantities during spore development (26). In Anabaena cylindrica, a cyanobacterium, a storage polypeptide has been identified that is sequestered during spore formation and stationary phase cultures (27,28). In both cases, the function of the storage proteins is similar to that of seeds, providing a readily accessible source of nitrogen upon the resumption of growth.Lower vascular plants also have been shown to contain storage proteins. Reports have described storage protein decline in fern spores during imbibition and germination (22,24). However, since no fern spore storage proteins have been isolated and characterized, the developmental role of these proteins remains unclear.Gymnosperms, a group that contains many higher vascular plants of ancient lineage, contain seed storage proteins within haploid megagametophyte tissue. While investigators have identified storage proteins in various pine species (13, 18), only in the cycad, Macrozamia communis, has gymnosperm storage protein been isolated and partially characterized (1).Clearly more work is required with primitive plant groups in order to determine whether the formation of ancestral storage protein genes occurred before higher vascular plants arose. This paper describes research concerned with the identification, partial characterization, and localization of the principal storage proteins in the spores of the ostrich fern, Matteuccia struthiopteris. The qualitative and quantitative data presented here indicate that fern spores have protein bodies containing globulin storage proteins that are biochemically similar to certain angiosperm seed storage proteins. MATERIALS AND METHODSPlant Material. Mature fertile leaves of Matteuccia struthiopteris (L.) Todaro were collected from several locations in Hanover, NH, in late autumn and spores were released by repeatedly soaking the leaves in water and then drying them at room temperature. Spores were separated from associated organic debris using an Allen Bradley sonic sifter and stored in dark bottles at 4°C. For germination time course studies, 200 mg spores were placed in 100 ml of distilled H20 in a 1-L Erlenmeyer flask and maintained on a 12 h light-dark cycle at 25°C in a growth chamber. Illumination (250 ft-c = 40 AE...

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“…The amino acid sequences of these proteins are known, and those of SASP A and C are extremely similar, whereas that of SASP B is much less closely related (14)(15)(16)(17). This system appears even more complex at the gene level because, in addition to the genes coding for SASP A and C, there are five other genes that code for proteins with amino acid sequences extremely similar (70 to 90% sequence identity) to those of SASP A and C (7)(8)(9). All of these closely related SASP Aand C-like genes are expressed in parallel midway in sporulation, although some (SASP A and C genes) are expressed at much higher levels than others (7)(8)(9).…”

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“…We decided to use this approach for two reasons. (i) Previous work had strongly suggested that SASP genes would not be transcribed in Escherichia coli from their own promoters (4,14), and (ii) several SASP genes, even if transcribed in E. coli, are either translated very poorly or the final protein is unstable (3,7,9,14). DNA (17).…”

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“…DNA (17). Each digest was electrophoresed on a 1% agarose gel, and DNA fragments of 0.5 to 2 kilobases (kb) were isolated as previously described (9). The pooled fractionated DNA (-50 ,ug) was mixed with a 27-fold molar excess of a mixture of EcoRI linkers; this linker mixture contained an equimolar mixture of the 8-, 10-, and 12-mer EcoRI linkers (each obtained from New England BioLabs) to ensure that we would obtain the SASP B gene in frame with the lacZ gene of Xgtll.…”

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Cloning and nucleotide sequence of the Bacillus megaterium gene coding for small, acid-soluble spore protein B

Hackett¹,

Setlow²,

Setlow³

1986

J Bacteriol

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The Bacillus megaterium gene coding for small, acid-soluble spore protein (SASP) B was cloned and its nucleotide sequence was determined. The amino acid sequence predicted from the DNA sequence was identical to that determined previously for SASP B, with the exception of the amino-terminal methionine predicted from the gene sequence which is presumably removed posttranslationally and an asparagine residue predicted at position 21 which was originally identified as an aspartate residue. The mRNA encoded by the SASP B gene is synthesized for only a discrete period midway in sporulation, in parallel with mRNAs coding for other SASPs. The small size of the SASP B mRNA (365 nucleotides) indicated that the mRNA is monocistronic. The SASP B gene itself hybridized strongly to only one band in Southern blots of restriction enzyme digests of B. megaterium DNA, suggesting that the SASP B gene is not a member of a highly conserved multigene family, as is the case for other SASP genes.

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Genes for Bacillus megaterium small, acid-soluble spore proteins: nucleotide sequence of two genes and their expression during sporulation

Cited by 22 publications

References 13 publications

Genes for Bacillus megaterium small, acid-soluble spore proteins: cloning and nucleotide sequence of three additional genes from this multigene family

Genes for Bacillus megaterium small, acid-soluble spore proteins: cloning and nucleotide sequence of three additional genes from this multigene family

Biochemistry of Fern Spore Germination: Globulin Storage Proteins in Matteuccia struthiopteris L.

Cloning and nucleotide sequence of the Bacillus megaterium gene coding for small, acid-soluble spore protein B

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