Evidence map›Paper›PMID 34112860›Full record

ArticleScientific reports2021

Genome-wide characterization of peptidyl-prolyl cis-trans isomerases in Penicillium and their regulation by salt stress in a halotolerant P. oxalicum.

Mangaljeet Singh, Kirandeep Kaur, Avinash Sharma, Rajvir Kaur, Dimple Joshi, Megha Chatterjee, Iman Dandapath, Amarjeet Kaur, Harpreet Singh, Prabhjeet Singh

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 14 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Mangaljeet SinghDepartment of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Kirandeep Kaur *Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Avinash Sharma *Department of Microbiology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Rajvir Kaur *Department of Microbiology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Dimple Joshi *Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Megha Chatterjee *Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Iman Dandapath *Department of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Amarjeet KaurDepartment of Microbiology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India.
Harpreet SinghDepartment of Bioinformatics, Hans Raj Mahila Maha Vidyalaya, Jalandhar, Punjab, 144008, India.
Prabhjeet SinghDepartment of Biotechnology, Guru Nanak Dev University, Amritsar, Punjab, 143005, India. singhprabhjeet62@gmail.com.
Guru Nanak Dev University · INHans Raj Mahila Maha Vidyalaya · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidyl-prolyl cis-trans isomerases (PPIases) are the only class of enzymes capable of cis-trans isomerization of the prolyl peptide bond. The PPIases, comprising of different families viz., cyclophilins, FK506-binding proteins (FKBPs), parvulins and protein phosphatase 2A phosphatase activators (PTPAs), play essential roles in different cellular processes. Though PPIase gene families have been characterized in different organisms, information regarding these proteins is lacking in Penicillium species, which are commercially an important fungi group. In this study, we carried out genome-wide analysis of PPIases in different Penicillium spp. and investigated their regulation by salt stress in a halotolerant strain of Penicillium oxalicum. These analyses revealed that the number of genes encoding cyclophilins, FKBPs, parvulins and PTPAs in Penicillium spp. varies between 7-11, 2-5, 1-2, and 1-2, respectively. The halotolerant P. oxalicum depicted significant enhancement in the mycelial PPIase activity in the presence of 15% NaCl, thus, highlighting the role of these enzymes in salt stress adaptation. The stress-induced increase in PPIase activity at 4 and 10 DAI in P. oxalicum was associated with higher expression of PoxCYP18. Characterization of PPIases in Penicillium spp. will provide an important database for understanding their cellular functions and might facilitate their applications in industrial processes through biotechnological interventions.

Indexed as

Amino Acid SequenceCatalysisCyclophilinsGene Expression Regulation, FungalGenome, FungalNIMA-Interacting Peptidylprolyl IsomerasePenicilliumPeptidylprolyl IsomerasePhosphoprotein PhosphatasesProtein FoldingTacrolimus Binding ProteinsCyclophilinsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphoprotein PhosphatasesTacrolimus Binding Proteins

Identifiers

PMID34112860
PMCPMC8192932
OpenAlexW3134527106

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.