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J. Biol. Chem., Vol. 277, Issue 18, 15293-15302, May 3, 2002
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From the Institute of Microbial Technology, Sector 39 A,
Chandigarh 160036, India
The truncated hemoglobins HbN and HbO of
Mycobacterium tuberculosis H37Rv share little sequence
similarity and display structural differences in their EF-loop regions,
suggesting distinct function(s) for these hemoglobins. HbO of M. tuberculosis was expressed in Escherichia coli and
Mycobacterium smegmatis as a 14.5-kDa homodimeric heme
protein exhibiting nearly 50-fold (P50 ~0.51)
lower oxygen affinity than HbN. 40-50% of HbO remained associated
with the cell membranes and significantly enhanced its respiration in
comparison with the membrane fractions of control cells or cells
overproducing HbN. Oxygen uptake of HbO-associated membranes was
decreased by washing and restored by adding HbO. Additionally, membrane
vesicles prepared from terminal oxidase-deficient
(cyo
Mycobacterium tuberculosis Hemoglobin HbO Associates
with Membranes and Stimulates Cellular Respiration of Recombinant
Escherichia coli*,
,
, cyd) mutants
of E. coli did not exhibit significant enhancement in oxygen uptake in the presence of HbO, suggesting its
interaction(s) with the electron transport chain. Expression of
HbO in Mycobacterium bovis bacillus Calmette-Guérin,
an experimental model of M. tuberculosis, was observed
(0.2-0.5% of total cellular proteins) throughout its aerobic growth.
These results provided evidence for the involvement of HbO with the
component of aerobic electron transport chain, suggesting that its
function may be related to the facilitation of oxygen transfer during
aerobic metabolism of M. tuberculosis. Membrane association
properties of HbO may thus play a crucial role in sequestering oxygen
and facilitating its availability to internalized M. tuberculosis (an obligate aerobe) under the hypoxic conditions of
its intracellular habitat.
*
This work was supported by the Department of Science and
Technology and the Council of Scientific and Industrial Research, India.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The on-line version of this article (available at
http://www.jbc.org) contains supplementary Table 1, which
has the NCBI and TIGR accession numbers of various truncated
hemoglobins included in Fig. 1, and Table 2, which shows the relative
percent similarity among various truncated hemoglobins.
Present address: National Bureau of Animal Genetic Resources,
Karnal 132001, India.
§
To whom correspondence should be addressed. Tel.: 91-172-695215;
Fax: 91-172-690632/690585; E-mail:
kanak@imtech.res.in.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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