Multidomain truncated hemoglobins: New members of the globin family exhibiting tandem repeats of globin units and domain fusion. Issue 7 (10th April 2017)
- Record Type:
- Journal Article
- Title:
- Multidomain truncated hemoglobins: New members of the globin family exhibiting tandem repeats of globin units and domain fusion. Issue 7 (10th April 2017)
- Main Title:
- Multidomain truncated hemoglobins: New members of the globin family exhibiting tandem repeats of globin units and domain fusion
- Authors:
- Hade, Mangesh Dattu
Kaur, Jagdeep
Chakraborti, Pradip K.
Dikshit, Kanak L. - Abstract:
- Abstract: Truncated hemoglobins (trHbs) are considered the most primitive members of globin superfamily and traditionally exist as a single domain heme protein in three distinct structural organizations, type I (trHb1_N), type II (trHb2_O) and type III (trHb3_P). Our search of microbial and lower eukaryotic genomes revealed a broad array of multidomain organization, representing multiunit and chimeric forms of trHbs, where multiple units of trHbs are joined together and/or integrated with distinct functional domains. Globin motifs of these multidomain trHbs were from all three groups of trHbs and unambiguously assigned to trHb1_N, trHb2_O and trHb3_P. Multiunit and chimeric forms of trHb1_N were identified exclusively in ciliated protozoan parasites, where multiple units of trHb are integrated in tandem and/or fused with another redox active or signalling domain, presenting an interesting example of gene duplication and fusion in lower eukaryotes. In contrast, trHb2_O and trHb3_P trHbs were found only in bacteria in two or multidomain organization, where amino or carboxy terminus of trHb unit is integrated with different redox‐active or oxidoreductase domains. The identification of these new multiunit and chimeric trHbs and their specific phyletic distribution presents an interesting and challenging finding to explore and understand complex functionalities of these novel multidomain trHbs. © 2017 IUBMB Life, 69(7):479–488, 2017
- Is Part Of:
- IUBMB life. Volume 69:Issue 7(2017)
- Journal:
- IUBMB life
- Issue:
- Volume 69:Issue 7(2017)
- Issue Display:
- Volume 69, Issue 7 (2017)
- Year:
- 2017
- Volume:
- 69
- Issue:
- 7
- Issue Sort Value:
- 2017-0069-0007-0000
- Page Start:
- 479
- Page End:
- 488
- Publication Date:
- 2017-04-10
- Subjects:
- truncated hemoglobins -- domain duplication -- domain fusion -- trHb1_N -- trHb2_O -- trHb3_P
Biochemistry -- Periodicals
Molecular biology -- Periodicals
572.8 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1521-6551 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/iub.1630 ↗
- Languages:
- English
- ISSNs:
- 1521-6543
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4588.826000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2901.xml