scholarly journals Mutational Analysis of the sbo-alb Locus of Bacillus subtilis: Identification of Genes Required for Subtilosin Production and Immunity

2000 ◽  
Vol 182 (11) ◽  
pp. 3266-3273 ◽  
Author(s):  
Guolu Zheng ◽  
Robin Hehn ◽  
Peter Zuber
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mutational Analysis ◽  
Sequence Data ◽  
Maturation Process ◽  
Coding Region ◽  
Anaerobic Conditions ◽  
Chemical Modifications ◽  
New Gene

ABSTRACT The Bacillus subtilis 168 derivative JH642 produces a bacteriocin, subtilosin, which possesses activity againstListeria monocytogenes. Inspection of the amino acid sequence of the presubtilosin polypeptide encoded by the genesboA and sequence data from analysis of mature subtilosin indicate that the precursor subtilosin peptide undergoes several unique and unusual chemical modifications during its maturation process. The genes of the sbo-alb operon are believed to function in the synthesis and maturation of subtilosin. Nonpolar mutations introduced into each of the alb genes resulted in loss or reduction of subtilosin production. sboA, albA, andalbF mutants showed no antilisterial activity, indicating that the products of these genes are critical for the production of active subtilosin. Mutations in albB, -C, and -D resulted in reduction of antilisterial activity and decreased immunity to subtilosin, particularly under anaerobic conditions. A new gene, sboX, encoding another bacteriocin-like product was discovered residing in a sequence overlapping the coding region of sboA. Construction of ansboX-lacZ translational fusion and analysis of its expression indicate that sboX is induced in stationary phase of anaerobic cultures of JH642. An in-frame deletion of thesboX coding sequence did not affect the antilisterial activity or production of or immunity to subtilosin. The results of this investigation show that the sbo-alb genes are required for the mechanisms of subtilosin synthesis and immunity.

scholarly journals cDNA nucleotide sequence encoding the ZPC protein of Australian hydromyine rodents: a novel sequence of the putative sperm-combining site within the family Muridae

Zygote ◽  
2002 ◽  
Vol 10 (4) ◽  
pp. 291-299 ◽  
Author(s):  
Christine A. Swann ◽  
Rory M. Hope ◽  
William G. Breed
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Amino Acid Sequence Identity ◽  
Sequence Data ◽  
Coding Region ◽  
Cdna Sequences ◽  
Sequence Identity ◽  
Murid Rodents

This comparative study of the cDNA sequence of the zona pellucida C (ZPC) glycoprotein in murid rodents focuses on the nucleotide and amino acid sequence of the putative sperm-combining site. We ask the question: Has divergence evolved in the nucleotide sequence of ZPC in the murid rodents of Australia? Using RT-PCR and (RACE) PCR, the complete cDNA coding region of ZPC in the Australian hydromyine rodents Notomys alexis and Pseudomys australis, and a partial cDNA sequence from a third hydromyine rodent, Hydromys chrysogaster, has been determined. Comparison between the cDNA sequences of the hydromyine rodents reveals that the level of amino acid sequence identity between N. alexis and P. australis is 96%, whereas that between the two species of hydromyine rodents and M. musculus and R. norvegicus is 88% and 87% respectively. Despite being reproductively isolated from each other, the three species of hydromyine rodents have a 100% level of amino acid sequence identity at the putative sperm-combining site. This finding does not support the view that this site is under positive selective pressure. The sequence data obtained in this study may have important conservation implications for the dissemination of immunocontraception directed against M. musculus using ZPC antibodies.

scholarly journals Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit.

1990 ◽  
Vol 265 (8) ◽  
pp. 4204-4209
Author(s):  
K Schott ◽  
J Kellermann ◽  
F Lottspeich ◽  
A Bacher
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Alpha Subunit

scholarly journals The Major Acid-soluble Proteins of Bacillus subtilis Spores: Partial Amino Acid Sequence and Forespore Location of Their mRNAs

Microbiology ◽  
1987 ◽  
Vol 133 (8) ◽  
pp. 2237-2246
Author(s):  
H. BLOM ◽  
R. MORSE ◽  
J. MANDELKORN ◽  
M. ARNAUD ◽  
R. WARBURG ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Soluble Proteins ◽  
Partial Amino Acid Sequence ◽  
Major Acid

scholarly journals Nucleotide and derived amino acid sequences of a cDNA coding for pre-uteroglobin from the lung of the hare (Lepus capensis)

1986 ◽  
Vol 235 (3) ◽  
pp. 895-898 ◽  
Author(s):  
M S López de Haro ◽  
A Nieto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Untranslated Regions ◽  
Coding Region ◽  
Homologous Proteins ◽  
Lepus Capensis ◽  
Rabbit Gene

An almost full-length cDNA coding for pre-uteroglobin from hare lung was cloned and sequenced. The derived amino acid sequence indicated that hare pre-uteroglobin contained 91 amino acids, including a signal peptide of 21 residues. Comparison of the nucleotide sequence of hare pre-uteroglobin cDNA with that previously reported for the rabbit gene indicated five silent point substitutions and six others leading to amino acid changes in the coding region. The untranslated regions of both pre-uteroglobin mRNAs were very similar. The amino acid changes observed are discussed in relation to the different progesterone-binding abilities of both homologous proteins.

Expression patterns of the genes that encode lectin or lectin-related polypeptides in Robinia pseudoacacia

1999 ◽  
Vol 26 (5) ◽  
pp. 495 ◽  
Author(s):  
Kazumasa Yoshida ◽  
Kiyoshi Tazaki
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Expression Patterns ◽  
Robinia Pseudoacacia ◽  
Regulation Of Expression ◽  
Nucleotide Sequence Data ◽  
Reading Frame ◽  
Inner Bark

Three genomic clones (Rplec2, Rplec5 and Rplec6) and a cDNA clone (LECRPA4) that encoded lectin or lectin-related polypeptides were isolated from Robinia pseudoacacia L. A comparison of the nucleotide sequences of Rplec2 and a previously reported cDNA for the subunit indicated that Rplec2 encoded the 29 kDa subunit of the inner-bark lectin RPbAI. Rplec5 encoded a polypeptide whose deduced amino acid sequence was 96.1% identical to that of a subunit of seed lectin. The amino acid sequence deduced from the open reading frame of Rplec6 showed 61.1% identity to that encoded by Rplec5. LECRPA4 was isolated from an inner bark cDNA library and appeared to encode the 26 kDa subunit of inner-bark lectin RPbAII. The expression patterns of the various genes in tissues were examined by the reverse transcriptase-polymerase chain reaction (RT-PCR) with appropriate primers. Rplec2 transcripts were detected in the inner bark and roots. Rplec5 transcripts were detected in the inner bark, seeds and roots. No Rplec6 transcripts were detected in all tissues examined. LECRPA4 transcripts were found in leaves and in the inner bark. The level of expression of Rplec2 in the inner bark appeared to be similar in samples collected in different years and from different trees, whereas levels of expression of Rplec5 and LECRPA4 varied. These results suggest the differential regulation of expression of members of the lectin gene family in tissues of R. pseudoacacia. The nucleotide sequence data reported herein will appear in the DDBJ, EMBL and GenBank Nucleotide Sequence Databases under the accession numbers AB 012632 (Rplec2), AB012633 (Rplec5), AB012634 (Rplec6) and AB012635 (LECRPA4).

scholarly journals Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17

Blood ◽  
1988 ◽  
Vol 72 (2) ◽  
pp. 593-600 ◽  
Author(s):  
JP Rosa ◽  
PF Bray ◽  
O Gayet ◽  
GI Johnston ◽  
RG Cook ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Chromosome 17 ◽  
Coding Region ◽  
Membrane Glycoproteins ◽  
Cdna Sequences ◽  
Hel Cells ◽  
Adhesive Proteins

Abstract Platelet aggregation requires the binding of adhesive proteins such as fibrinogen to the heterodimer of membrane glycoproteins IIb (GPIIb) and IIIa (GPIIIa). Human erythroleukemia (HEL) cells synthesize both GPIIb and GPIIIa. Using poly(A+) RNA purified from HEL cells, we constructed a cDNA library in the lambda gt10 phage vector. This library was screened with a 38mer oligonucleotide derived from a platelet GPIIIa peptide, and three overlapping cDNAs were isolated. The three inserts encompassed 3.5 kilobases (kb), including the entire coding region of mature GPIIIa (2,286 basepairs, bp) and 1.3 kb of 3′ untranslated sequence. All 222 residues determined directly from platelet GPIIIa tryptic peptides exactly matched the HEL cell-deduced amino acid sequence. The HEL cell sequence matched a previously reported endothelial cell cDNA sequence except for eight nucleotides. Five of these nucleotide differences were silent changes consistent with genetic polymorphisms. The other three differences resulted in changes in the deduced amino acid sequence of GPIIIa; reexamination of the endothelial cell cDNA sequence in these three areas revealed that it is actually identical to the HEL cell sequence. The virtual identity of the endothelial and HEL cell cDNA sequences provides direct evidence that GPIIIa is a subunit common to cell-adhesion receptors present in more than one cell type. We localized the gene for GPIIIa to chromosome 17, the same chromosome to which we had previously mapped the gene for GPIIb.

Sign in / Sign up

Export Citation Format

Share Document