Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Resuscitation
Promoting Factor (Rpf) domain of M. tuberculosis

1H, 15N and 13C Chemical Shifts Assignments of the Resuscitation Promoting
Factor domain of Rv1009 from Mycobacterium tuberculosis

Solution Structure Of A Resuscitation Promoting Factor Domain From Mycobacterium Tuberculosis

Crystal Structure Of The Resuscitation Promoting Factor Rpfb

putative resuscitation-promoting factor [Mycobacterium bovis BCG str. Tokyo 172]

Probable resuscitation-promoting factor rpfB [Mycobacterium tuberculosis H37Rv]

Probable resuscitation-promoting factor rpfB [Mycobacterium bovis AF2122/97]

Probable resuscitation-promoting factor rpfB [Mycobacterium bovis BCG str. Pasteur 1173P2]

conserved hypothetical protein [Mycobacterium tuberculosis CDC1551]

putative resuscitation-promoting factor RpfB [Mycobacterium tuberculosis H37Ra]

resuscitation-promoting factor rpfB [Mycobacterium tuberculosis F11]

resuscitation-promoting factor rpfB [Mycobacterium tuberculosis KZN 1435]

resuscitation-promoting factor rpfB [Mycobacterium tuberculosis C]

resuscitation-promoting factor rpfB [Mycobacterium tuberculosis H37Rv]

hypothetical protein MT1038 [Mycobacterium tuberculosis CDC1551]

resuscitation-promoting factor rpfB [Mycobacterium bovis AF2122/97]

Studies of starved Micrococcus luteus has led to the identification of a
secreted protein which resuscitated dormant cells allowing them to enter the
cell cycle. This factor was named resuscitation promoting factor (Rpf) and was
classified as the first bacterial cytokine (Mukamolova, Kaprelyants et al.
1998). Homologues of the rpf genes are widely distributed among the high G+C
cohort of Gram-positive bacteria including the Mycobacterial pathogens M.
tuberculosis and M. leprae (Mukamolova, Turapov et al. 2002). M. tuberculosis
can spend many years dormant in human tissue so the mechanism of revival of
dormant M. tuberculosis is of major medical interest. Knockout of the unique
rpf gene in M. luteus has showed to be lethal (Mukamolova, Turapov et al. 2002)
while in M. tuberculosis, which has five rpf genes, none of these individual
genes was found to be essential suggesting a functional redundancy (Tufariello,
Jacobs et al. 2004). However, in a genome wide transposon study the rpfB
knockout caused slowing of growth (Sassetti, Boyd et al. 2003) and all five rpf
homologues are expressed in M. tuberculosis obtained from
extended-stationary-phase cultures suggesting the possibility that Rpf may play
a role in the reactivation of quiescent bacilli. Recently, using sequence
analysis and homology modelling, we predicted that the structure of the common
domain of the Rpf proteins (~100 amino-acid) possess a lysozyme-like domain
(Cohen-Gonsaud, Keep et al. 2004).

A cryogenic probe equipped the 500 MHz spectrometer.