Transport of intact porphyrin by HpuAB, the hemoglobin-haptoglobin utilization system of Neisseria meningitidis

J Bacteriol. 1998 Nov;180(22):6043-7. doi: 10.1128/JB.180.22.6043-6047.1998.

Abstract

The meningococcal hemA gene was cloned and used to construct a porphyrin biosynthesis mutant. An analysis of the hemA mutant indicated that meningococci can transport intact porphyrin from heme (Hm), hemoglobin (Hb), and Hb-haptoglobin (Hp). By constructing a HemA- HpuAB- double mutant, we demonstrated that HpuAB is required for the transport of porphyrin from Hb and Hb-Hp.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aldehyde Oxidoreductases / genetics
  • Aldehyde Oxidoreductases / metabolism
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Base Sequence
  • Biological Transport
  • Carrier Proteins / metabolism*
  • DNA, Bacterial
  • Haptoglobins / metabolism*
  • Hemoglobins / metabolism*
  • Lipoproteins / genetics
  • Lipoproteins / metabolism
  • Molecular Sequence Data
  • Mutagenesis
  • Neisseria meningitidis / genetics
  • Neisseria meningitidis / metabolism*
  • Porphyrins / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Carrier Proteins
  • DNA, Bacterial
  • Haptoglobins
  • Hemoglobins
  • HpuB protein, Neisseria
  • Lipoproteins
  • Porphyrins
  • Aldehyde Oxidoreductases
  • glutamyl tRNA reductase

Associated data

  • GENBANK/AF067426
  • GENBANK/AF067427