Uptake of glycerol - 2 - phosphate via the ugp - encoded transporter in 1 Escherichia coli K 12 2 3 4

نویسندگان

  • Kechao Yang
  • Mi Wang
  • William W. Metcalf
چکیده

3 4 Kechao Yang, Mi Wang and William W. Metcalf* 5 6 Department of Microbiology, University of Illinois at Urbana-Champaign, B103 CLSL, 7 601 S. Goodwin, Urbana, IL 61801 8 9 *Corresponding Author: Department of Microbiology, University of Illinois at Urbana10 Champaign, 601 South Goodwin Avenue, Urbana, IL 61801, Phone: 217-244-1943, 11 Fax: 217-244-6697, email: [email protected] 12 13 1 Present Address: General Electric (China) Research and Development Center Co. Ltd, 14 No. 1800 Cailun Road, Shanghai 201203, China 15 16 Running title: glycerol-2-Pi transport in E. coli 17 18 Copyright © 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved. J. Bacteriol. doi:10.1128/JB.00235-09 JB Accepts, published online ahead of print on 8 May 2009

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

The pho regulon-dependent Ugp uptake system for glycerol-3-phosphate in Escherichia coli is trans inhibited by Pi.

sn-Glycerol-3-phosphate (G3P) or glyceryl phosphoryl phosphodiesters, the substrates of the phoB-dependent Ugp transport system, when transported exclusively through this system, can serve as a sole source of phosphate but not as a sole source of carbon (H. Schweizer, M. Argast, and W. Boos, J. Bacteriol. 150:1154-1163, 1982). In order to explain this phenomenon, we tested two possibilities: re...

متن کامل

Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli.

The periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli transport sn-glycerol-3-phosphate and maltose, respectively. The UgpC and MalK proteins of these transport systems, which couple energy to the transport process by ATP-hydrolysis, are highly homologous, suggesting that they might be functionally exchangeable. Complementation experiments showed that UgpC ...

متن کامل

Purification and characterization of glpX-encoded fructose 1, 6-bisphosphatase, a new enzyme of the glycerol 3-phosphate regulon of Escherichia coli.

In Escherichia coli, gene products of the glp regulon mediate utilization of glycerol and sn-glycerol 3-phosphate. The glpFKX operon encodes glycerol diffusion facilitator, glycerol kinase, and as shown here, a fructose 1,6-bisphosphatase that is distinct from the previously described fbp-encoded enzyme. The purified enzyme was dimeric, dependent on Mn(2+) for activity, and exhibited an apparen...

متن کامل

High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter.

The glycerol-3-phosphate (G3P) transporter, GlpT, from Escherichia coli mediates G3P and inorganic phosphate exchange across the bacterial inner membrane. It possesses 12 transmembrane alpha-helices and is a member of the Major Facilitator Superfamily. Here we report overexpression, purification, and characterization of GlpT. Extensive optimization applied to the DNA construct and cell culture ...

متن کامل

Crystal structure and mechanism of GlpT, the glycerol-3-phosphate transporter from E. coli.

The major facilitator superfamily represents the largest group of secondary active membrane transporters in prokaryotic and eukaryotic cells. They transport a vast variety of substrates, presumably via similar mechanisms, yet the details of these mechanisms remain unclear. Here we report the 3.3 A resolution structure of a member of this superfamily--GlpT, the glycerol-3-phosphate transporter f...

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:

دوره   شماره 

صفحات  -

تاریخ انتشار 2009