The ntp operon encoding the Na+V-ATPase of the thermophile Caloramator fervidus

Trees Ubbink-Kok; Jeroen Nijland; Dirk-Jan Slotboom; Juke S. Lolkema

doi:10.1007/s00203-006-0165-x

The ntp operon encoding the Na+V-ATPase of the thermophile Caloramator fervidus

Trees Ubbink-Kok, Jeroen Nijland, Dirk-Jan Slotboom, Juke S. Lolkema^*

^*Bijbehorende auteur voor dit werk

Onderzoeksoutput › Academic › peer review

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The V-type ATPase of the thermophile Caloramator fervidus is an ATP-driven Na+ pump. The nucleotide sequence of the ntpFIKECGABD operon containing the structural genes coding for the nine subunits of the enzyme complex was determined. The identity of the proteins in two pairs of subunits (D, E and F, G) that have very similar mobilities on SDS-PAGE of the purified complex (24.3 and 22.7 kDa, and 12.3 and 11.6 kDa) was established by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides.

Originele taal-2	English
Pagina's (van-tot)	513-517
Aantal pagina's	5
Tijdschrift	Archives of Microbiology
Volume	186
Nummer van het tijdschrift	6
DOI's	https://doi.org/10.1007/s00203-006-0165-x
Status	Published - dec-2006

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10.1007/s00203-006-0165-x

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title = "The ntp operon encoding the Na+V-ATPase of the thermophile Caloramator fervidus",

abstract = "The V-type ATPase of the thermophile Caloramator fervidus is an ATP-driven Na+ pump. The nucleotide sequence of the ntpFIKECGABD operon containing the structural genes coding for the nine subunits of the enzyme complex was determined. The identity of the proteins in two pairs of subunits (D, E and F, G) that have very similar mobilities on SDS-PAGE of the purified complex (24.3 and 22.7 kDa, and 12.3 and 11.6 kDa) was established by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides.",

keywords = "ntp Operon, V-ATPase, thermophile, Caloramator fervidus, molecular motor, central stalk, BACTERIUM CLOSTRIDIUM FERVIDUS, V-TYPE ATPASE, ELECTRON-MICROSCOPY, THERMUS-THERMOPHILUS, SUBUNIT ARRANGEMENT, ENTEROCOCCUS-HIRAE, PERIPHERAL STALK, STATOR STRUCTURE, COMPLEX, PURIFICATION",

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T1 - The ntp operon encoding the Na+V-ATPase of the thermophile Caloramator fervidus

AU - Ubbink-Kok, Trees

AU - Nijland, Jeroen

AU - Slotboom, Dirk-Jan

AU - Lolkema, Juke S.

PY - 2006/12

Y1 - 2006/12

N2 - The V-type ATPase of the thermophile Caloramator fervidus is an ATP-driven Na+ pump. The nucleotide sequence of the ntpFIKECGABD operon containing the structural genes coding for the nine subunits of the enzyme complex was determined. The identity of the proteins in two pairs of subunits (D, E and F, G) that have very similar mobilities on SDS-PAGE of the purified complex (24.3 and 22.7 kDa, and 12.3 and 11.6 kDa) was established by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides.

AB - The V-type ATPase of the thermophile Caloramator fervidus is an ATP-driven Na+ pump. The nucleotide sequence of the ntpFIKECGABD operon containing the structural genes coding for the nine subunits of the enzyme complex was determined. The identity of the proteins in two pairs of subunits (D, E and F, G) that have very similar mobilities on SDS-PAGE of the purified complex (24.3 and 22.7 kDa, and 12.3 and 11.6 kDa) was established by tryptic digestion of the protein bands followed by mass spectrometric analysis of the peptides.

KW - ntp Operon

KW - V-ATPase

KW - thermophile

KW - Caloramator fervidus

KW - molecular motor

KW - central stalk

KW - BACTERIUM CLOSTRIDIUM FERVIDUS

KW - V-TYPE ATPASE

KW - ELECTRON-MICROSCOPY

KW - THERMUS-THERMOPHILUS

KW - SUBUNIT ARRANGEMENT

KW - ENTEROCOCCUS-HIRAE

KW - PERIPHERAL STALK

KW - STATOR STRUCTURE

KW - COMPLEX

KW - PURIFICATION

U2 - 10.1007/s00203-006-0165-x

DO - 10.1007/s00203-006-0165-x

M3 - Article

VL - 186

SP - 513

EP - 517

JO - Archives of Microbiology

JF - Archives of Microbiology

SN - 0302-8933

IS - 6

ER -