Overexpression of bacterial hemoglobin causes incorporation of pre-beta-lactamase into cytoplasmic inclusion bodies.

نویسندگان

  • U Rinas
  • J E Bailey
چکیده

The expression of Vitreoscilla hemoglobin (VHb) in Escherichia coli JM101 (pRED2) causes the incorporation of the TEM beta-lactamase precursor into cytoplasmic inclusion bodies (IBs). Less pre-beta-lactamase is translocated and processed to its mature, periplasmic form in the strain coexpressing VHb than in the control strain E. coli JM101(pUC19) not expressing VHb. When cells are grown in a special fed-batch procedure, the formation of cytoplasmic IBs consisting of pre-beta-lactamase is also inducible in the control strain. Comparative microscopic and compositional analyses of IBs generated in E. coli JM101(pUC19) and JM101(pRED2) under identical growth conditions strongly suggest that pre-beta-lactamase and VHb coaggregate into common IBs in E. coli JM101 (pRED2).

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

Bacterial Overexpression of the Human Interleukin-2 in Insoluble Form via the pET Trx Fusion System

Selection of a system for successful recombinant protein production is important. The aim of this study wasto produce high levels of human interleukin-2 (hIL-2) in soluble form. To this end, the pET32a vector inEscherichia coli BL21 (DE3) was used as an expression system, since it was previously used for the productionof mouse IL-2 in soluble form. The results indicated that c...

متن کامل

Protein aggregation as bacterial inclusion bodies is reversible.

Inclusion bodies are refractile, intracellular protein aggregates usually observed in bacteria upon targeted gene overexpression. Since their occurrence has a major economical impact in protein production bio-processes, in vitro refolding strategies are under continuous exploration. In this work, we prove spontaneous in vivo release of both beta-galactosidase and P22 tailspike polypeptides from...

متن کامل

Production and Partial Purification of the Grapevine Fanleaf Virus Coat Protein 42 Polyclonal Antibody Against Inclusion Body Expressed in Escherichia coli

Background: Expression of virus coat protein (CP) in Escherichia coli often leads to production of partially folded aggregated proteins which are called inclusion bodies. Grapevine fanleaf virus (GFLV) is one of the most serious and widespread grapevine virus diseases around the world and in Iran.Objective: The main objective of this study was to find a s...

متن کامل

Optimized Cytoplasmic Expression of Water Soluble Human Thrombopoietin in Modified Bacterial Strain

Background: Thrombopoietin is a glycoprotein produced by liver and kidney which is responsible for regulating the platelet production. Thrombopoietin is a key ligand with impact on regulating the self-renewal of Hematopoietic stem cells and the regulation of Megakaryocytes progenitors. Previous studies have indicated that only N-terminal domain of this protein has receptor promoting ability. Th...

متن کامل

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized beta-sheet-rich aggre...

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:
  • Applied and environmental microbiology

دوره 59 2  شماره 

صفحات  -

تاریخ انتشار 1993