نتایج جستجو برای: periplasm

تعداد نتایج: 3548  

Journal: :Applied and environmental microbiology 2008
Lien Callewaert Lise Vanderkelen Daphne Deckers Abram Aertsen Johan Robben Chris W Michiels

A reverse zymogram method for the detection of bacterial lysozyme inhibitors was developed. This method was validated by using a periplasmic protein extract of Escherichia coli containing a known inhibitor and subsequently led to the detection of a new proteinaceous hen egg white lysozyme inhibitor in Proteus mirabilis.

Journal: :Biotechnology progress 1999
C P Chou J H Tseng B Y Kuo K M Lai M I Lin H K Lin

The effect of SecB chaperone on production of periplasmic penicillin acylase (PAC) in Escherichia coli was investigated. It appears that formation of PAC required the function of SecB chaperone and the amount of SecB required was at a basal level. The secB mutant was defective in production of PAC, and the impairment could be complemented by extrachromosomally supplementing SecB in trans. The f...

1992
M Villarejo HARRY H. YIM

coli. encodes a periplasmic protein in Escherichia osmY, a new hyperosmotically inducible gene,

Journal: :Applied and environmental microbiology 2013
Cristina Sánchez Manabu Itakura Hisayuki Mitsui Kiwamu Minamisawa

To understand the mechanisms underlying the increased N2O reductase activity in the Bradyrhizobium japonicum 5M09 mutant from enrichment culture under N2O respiration, we analyzed the expression of genes encoding denitrification reductases and regulators. Our results suggest a common regulation of nap (encoding periplasmic nitrate reductase) and nos (encoding N2O reductase).

Journal: :Journal of bacteriology 2005
Nico Nouwen Magdalena Piwowarek Greetje Berrelkamp Arnold J M Driessen

A remarkable feature of proteins of the SecD and SecF family involved in protein translocation is that they possess a very large first periplasmic domain. Here we report that this large first periplasmic domain is not required for the SecD-SecF interaction but that it is important for catalyzing protein translocation.

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Natalie A Dye Zachary Pincus Julie A Theriot Lucy Shapiro Zemer Gitai

The actin homolog MreB contributes to bacterial cell shape. Here, we explore the role of the coexpressed MreC protein in Caulobacter and show that it forms a periplasmic spiral that is out of phase with the cytoplasmic MreB spiral. Both mreB and mreC are essential, and depletion of either protein results in a similar cell shape defect. MreB forms dynamic spirals in MreC-depleted cells, and MreC...

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