Characterization of IS1167, a New Insertion Sequence in Streptococcus pneumoniae

Plasmid ◽  
1995 ◽  
Vol 33 (2) ◽  
pp. 127-138 ◽  
Author(s):  
Lixin Zhou ◽  
Francis M. Hui ◽  
Donald A. Morrison
Keyword(s):  
Streptococcus Pneumoniae ◽  
Insertion Sequence

scholarly journals Characterization of IS1515, a Functional Insertion Sequence in Streptococcus pneumoniae

1998 ◽  
Vol 180 (6) ◽  
pp. 1381-1388 ◽  
Author(s):  
Rosario Muñoz ◽  
Rubens López ◽  
Ernesto García
Keyword(s):  
Streptococcus Pneumoniae ◽  
Insertion Sequence ◽  
Frameshift Mutation ◽  
Lactobacillus Helveticus ◽  
Inverted Repeats ◽  
Insertion Sequences ◽  
Amino Acid Residues ◽  
Streptomyces Albus

ABSTRACT We describe the characterization of a new insertion sequence, IS1515, identified in the genome of Streptococcus pneumoniae I41R, an unencapsulated mutant isolated many years ago (R. Austrian, H. P. Bernheimer, E. E. B. Smith, and G. T. Mills, J. Exp. Med. 110:585–602, 1959). A copy of this element located in the cap1E I41R gene was sequenced. The 871-bp-long IS1515 element possesses 12-bp perfect inverted repeats and generates a 3-bp target duplication upon insertion. The IS encodes a protein of 271 amino acid residues similar to the putative transposases of other insertion sequences, namely IS1381 from S. pneumoniae, ISL2from Lactobacillus helveticus, IS702 from the cyanobacterium Calothrix sp. strain PCC 7601, and IS112 from Streptomyces albus G. IS1515 appears to be present in the genome of most type 1 pneumococci in a maximum of 13 copies, although it has also been found in the chromosome of pneumococcal isolates belonging to other serotypes. We have found that the unencapsulated phenotype of strain I41R is the result of both the presence of an IS1515 copy and a frameshift mutation in the cap1E I41Rgene. Precise excision of the IS was observed in the type 1 encapsulated transformants isolated in experiments designed to repair the frameshift. These results reveal that IS1515 behaves quite differently from other previously described pneumococcal insertion sequences. Several copies of IS1515 were also able to excise and move to another locations in the chromosome ofS. pneumoniae. To our knowledge, this is the first report of a functional IS in pneumococcus.

Phenotypic and genotypic characterization of Streptococcus pneumoniae resistant to macrolide in Casablanca, Morocco

2016 ◽  
Vol 40 ◽  
pp. 200-204 ◽  
Author(s):  
Idrissa Diawara ◽  
Khalid Zerouali ◽  
Khalid Katfy ◽  
Abouddihaj Barguigua ◽  
Houria Belabbes ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Genotypic Characterization ◽  
Phenotypic And Genotypic Characterization

Insertion Sequence Based Molecular Characterization of Burkholderia mallei NCTC 3709 Strain

2014 ◽  
Vol 38 (2) ◽  
pp. 99-102
Author(s):  
Chandan Prakash ◽  
P. Das ◽  
B. V. Sunil Kumar ◽  
Bincy Joseph ◽  
Vidya Singh ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Insertion Sequence ◽  
Burkholderia Mallei

scholarly journals Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family

2006 ◽  
Vol 394 (3) ◽  
pp. 575-579 ◽  
Author(s):  
Sergey V. Novoselov ◽  
Deame Hua ◽  
Alexey V. Lobanov ◽  
Vadim N. Gladyshev
Keyword(s):  
Mammalian Cells ◽  
Insertion Sequence ◽  
Phylogenetic Analyses ◽  
Dependent Manner ◽  
Putative Active Site ◽  
A Genome ◽  
Sequence Elements ◽  
Identification And Characterization ◽  
Insertion Sequence Elements

Sec (selenocysteine) is a rare amino acid in proteins. It is co-translationally inserted into proteins at UGA codons with the help of SECIS (Sec insertion sequence) elements. A full set of selenoproteins within a genome, known as the selenoproteome, is highly variable in different organisms. However, most of the known eukaryotic selenoproteins are represented in the mammalian selenoproteome. In addition, many of these selenoproteins have cysteine orthologues. Here, we describe a new selenoprotein, designated Fep15, which is distantly related to members of the 15 kDa selenoprotein (Sep15) family. Fep15 is absent in mammals, can be detected only in fish and is present in these organisms only in the selenoprotein form. In contrast with other members of the Sep15 family, which contain a putative active site composed of Sec and cysteine, Fep15 has only Sec. When transiently expressed in mammalian cells, Fep15 incorporated Sec in an SECIS- and SBP2 (SECIS-binding protein 2)-dependent manner and was targeted to the endoplasmic reticulum by its N-terminal signal peptide. Phylogenetic analyses of Sep15 family members suggest that Fep15 evolved by gene duplication.

scholarly journals Structural and Enzymatic Characterization of the Choline Kinase LicA from Streptococcus pneumoniae

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0120467 ◽  
Author(s):  
Lei Wang ◽  
Yong-Liang Jiang ◽  
Jing-Ren Zhang ◽  
Cong-Zhao Zhou ◽  
Yuxing Chen
Keyword(s):  
Streptococcus Pneumoniae ◽  
Choline Kinase ◽  
Enzymatic Characterization

scholarly journals Identification and characterization of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae

2001 ◽  
Vol 355 (2) ◽  
pp. 431 ◽  
Author(s):  
Daniel R. SYLVESTER ◽  
Emilio ALVAREZ ◽  
Arun PATEL ◽  
Kapila RATNAM ◽  
Howard KALLENDER ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Gram Positive ◽  
Identification And Characterization

scholarly journals Kinetic Characterization of the WalRKSpn (VicRK) Two-Component System of Streptococcus pneumoniae: Dependence of WalKSpn (VicK) Phosphatase Activity on Its PAS Domain

2010 ◽  
Vol 192 (9) ◽  
pp. 2346-2358 ◽  
Author(s):  
Alina D. Gutu ◽  
Kyle J. Wayne ◽  
Lok-To Sham ◽  
Malcolm E. Winkler
Keyword(s):  
Amino Acids ◽  
Streptococcus Pneumoniae ◽  
Phosphatase Activity ◽  
Pas Domain ◽  
Kinetic Characterization ◽  
Two Component System ◽  
Histidine Kinases ◽  
Component System ◽  
Two Component

ABSTRACT The WalRK two-component system plays important roles in maintaining cell wall homeostasis and responding to antibiotic stress in low-GC Gram-positive bacteria. In the major human pathogen, Streptococcus pneumoniae, phosphorylated WalR Spn (VicR) response regulator positively controls the transcription of genes encoding the essential PcsB division protein and surface virulence factors. WalR Spn is phosphorylated by the WalK Spn (VicK) histidine kinase. Little is known about the signals sensed by WalK histidine kinases. To gain information about WalK Spn signal transduction, we performed a kinetic characterization of the WalRK Spn autophosphorylation, phosphoryltransferase, and phosphatase reactions. We were unable to purify soluble full-length WalK Spn . Consequently, these analyses were performed using two truncated versions of WalK Spn lacking its single transmembrane domain. The longer version (Δ35 amino acids) contained most of the HAMP domain and the PAS, DHp, and CA domains, whereas the shorter version (Δ195 amino acids) contained only the DHp and CA domains. The autophosphorylation kinetic parameters of Δ35 and Δ195 WalK Spn were similar [Km (ATP) ≈ 37 μM; k cat ≈ 0.10 min−1] and typical of those of other histidine kinases. The catalytic efficiency of the two versions of WalK Spn ∼P were also similar in the phosphoryltransfer reaction to full-length WalR Spn . In contrast, absence of the HAMP-PAS domains significantly diminished the phosphatase activity of WalK Spn for WalR Spn ∼P. Deletion and point mutations confirmed that optimal WalK Spn phosphatase activity depended on the PAS domain as well as residues in the DHp domain. In addition, these WalK Spn DHp domain and ΔPAS mutations led to attenuation of virulence in a murine pneumonia model.

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