The location of N-acetylgalactosamine in the walls of Bacillus subtilis 168.

نویسندگان

  • M Duckworth
  • A R Archibald
  • J Baddiley
چکیده

The N-acetylgalactosamine in the walls of Bacillus subtilis 168 occurs in two polymers. One of these contains N-acetylgalactosamine, glucose and phosphorus and is attached to the peptidoglycan through an alkali-labile bond; preliminary studies indicate that a repeating unit of this polymer is glucosyl-N-acetylgalactosamine 1-phosphate. N-Acetylgalactosamine is also associated with the peptidoglycan in a component that is not converted into the free sugar or other soluble compounds on treatment of the walls with alkali. The two polymers containing N-acetylgalactosamine are released on autolysis of the walls and can be separated by ion-exchange chromatography. As glucose 6-phosphate is produced by gentle hydrolysis of the wall with acid a third phosphate polymer, poly(glucose 1-phosphate), may occur in this wall. However, as no polymer with this structure could be separated from that containing galactosamine, its existence has not been established unequivocally. The methods described permit the study of variations in N-acetylgalactosamine content with respect to growth conditions.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Poly(glucosyl-N-acetylgalactosamine 1-phosphate), a wall teichoic acid of Bacillus subtilis 168: its biosynthetic pathway and mode of attachment to peptidoglycan.

The ggaAB operon of Bacillus subtilis 168 encodes enzymes responsible for the synthesis of poly(glucosyl N-acetylgalactosamine 1-phosphate) [poly(GlcGalNAc 1-P)], a wall teichoic acid (WTA). Analysis of the nucleotide sequence revealed that both GgaA and GgaB contained the motif characteristic of sugar transferases, while GgaB was most likely to be bifunctional, being endowed with an additional...

متن کامل

tagO is involved in the synthesis of all anionic cell-wall polymers in Bacillus subtilis 168.

Sequence homologies suggest that the Bacillus subtilis 168 tagO gene encodes UDP-N-acetylglucosamine:undecaprenyl-P N-acetylglucosaminyl 1-P transferase, the enzyme responsible for catalysing the first step in the synthesis of the teichoic acid linkage unit, i.e. the formation of undecaprenyl-PP-N-acetylglucosamine. Inhibition of tagO expression mediated by an IPTG-inducible P(spac) promoter le...

متن کامل

The lytE gene of Bacillus subtilis 168 encodes a cell wall hydrolase.

Bacillus subtilis cell wall-bound protein CWBP33 is encoded by lytE, a gene expressed during the exponential growth phase. Sequence analysis of LytE, a 33-kDa protein, reveals two domains. The N-terminal domain contains a threefold-repeated motif common to several peptidoglycan binding proteins, while the C-terminal domain, probably carrying the catalytic activity, has homology with certain exo...

متن کامل

Regulation of the bacterial cell wall: analysis of a mutant of Bacillus subtilis defective in biosynthesis of teichoic acid.

Bacillus subtilis 168ts-200B is a temperature-sensitive mutant of B. subtilis 168 which grows as rods at 30 C but as irregular spheres at 45 C. Growth at the nonpermissive temperature resulted in a deficiency of teichoic acid in the cell wall. A decrease in teichoic acid synthesis coupled with the rapid turnover of this polymer led to a progressive loss until less than 20% of the level found in...

متن کامل

Estimation of metabolizable energy equivalency of Bacillus Subtilis spore for male broiler chickens

There are many studies on the effects of probiotics on performance of broiler chickens, but none of them has evaluated the metabolizable energy (ME) equivalency values of probiotics. The aim of this study was to determine the metabolizable energy equivalency value of Bacillus subtilis spore and its potential for decreasing feed ME content and cost. One hundred seventy-six day-old male broilers ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Biochemical journal

دوره 130 3  شماره 

صفحات  -

تاریخ انتشار 1972